Growth Factors CD Antigens Enzymes Viral Antigens Recombinant Proteins Natural Proteins Monoclonal Antibodies Cytokines Polyclonal Antibodies Neurotrophins Chemokines Hormones Custom Antibodies Modified Histone Antibodies Tag/Control Antibodies Antibody Pairs Secondary Antibodies Small Molecular Antibodies Recombinant Antibodies ChIP Antibodies

Recombinant Proteins

Other

Calcium Binding Protein

Dynactin

Killer Cell Lectin-like Receptor

Dynein Light Chain

SNRP

Kirsten Rat Sarcoma Viral Oncogene

Dysbindin

Kruppel-Like Factor

Ectodysplasin

Elongator Acetyltransferase Complex

Endothelial Cell-Specific Molecule 1

Endoplasmic Reticulum Protein

Solute Carrier Family

Lactoferrin

EPH Receptor

Sorting Nexin

Calcyphosine

Leukocyte Cell Derived Chemotaxin

RAN Binding Protein

Calmodulin

Outer Membrane Protein

Ephrin

p53

sRAGE

Leukocyte-Associated Ig-Like Receptor

Paired Box

Parkinson Disease Protein

SPSB

LIN Protein

Parvalbumin

PCNA

SPARC

PDZ Domain Containing

LBP

Calpain

Calponin

Pentraxin

SRY (Sex Determining Region Y)-Box

Calreticulin

Eukaryotic Translation Initiation Factor

Peroxisomal Biogenesis Factor

Listeriolysin

Stathmin

PHD Finger Protein

LRG1

Calumenin

Phosducin-Like

Streptavidin Proteins

Candida Albicans

Phosphatase and Tensin

Lymphocyte Antigen

PITPN

Canopy FGF Signaling Regulator

Lysosomal-Associated Membrane Protein

Phospholipid Scramblase

STIP

Capping Protein

PIH1 Domain Containing

Pim Oncogene

SDHAF

CEA

Polymerase (RNA) (DNA directed) Polypeptide

MAD2

Superoxide Dismutase

Mago-Nashi Homolog

HLA

KCTD

Caspase Recruitment Domain Family

CEBP

Surfeit

POU Class

Synaptobrevin

ERCC

CCR4-NOT Transcription Complex

Exosome Component

Maltose Binding Protein

Prefoldin

Cell Division Cycle

Mediator Complex

FABP

Melanoma Antigen Family A

Synaptosomal Associated Protein

Pregnancy Specific Beta-1-Glycoprotein

Cellular Retinoic Acid Binding Protein

Centrin

Synaptotagmin

Member RAS Oncogene Family

Centromere Protein

Prion Protein

Processing Of Precursor

Syndecan

Profilin

Charged Multivesicular Body Protein

Programmed Cell Death

Chloride Intracellular Channel

Family with Sequence Similarity

Chromatin Modifying Protein

Synovial Sarcoma, X Breakpoint

Chromobox

Prohibitin

Syntaxin

F-Box Protein

Proprotein Convertase Subtilisin/Kexin

Chromogranin

Protein C-Ets

Ferritin

Protein Phosphatase

Fibrinogen

Protein-A, A/G & G

Chromosome Open Reading Frame

Fibronectin Type III Domain Containing

Synuclein

Folate Receptor

Four And A Half LIM

Fragile Histidine Triad

G Antigen

GABA(A) Receptor-Associated Protein

Gastrokine

Tachykinin

TAR DNA

Clathrin

GDP Dissociation Inhibitor

Prothymosin

Coagulation Factors

General Transcription Factor

RAD51

TBC1 Domain Family

RASSF

TCL

Ras-Related C3 Botulinum Toxin Substrate

GIPC PDZ Domain

Cofilin

TTC

Gliadin

Mesoderm Development Candidate

Coiled-Coil Domain

Receptor Activity-Modifying Protein

Met Proto-Oncogene

Glycophorin

Toll Like Receptor

Methylmalonic Aciduria

Regenerating Islet-Derived

THAP Domain

MHC class I chain-related gene

Glycoprotein Nmb

Collagen

Thioredoxin

Glypican

Microfibrillar Associated Protein

Actin

Regulator of Calcineurin

Gremlin

Regulator of G-Protein Signaling

Microtubule-Associated Protein

GTPase IMAP Family

Adaptor-Related Protein Complex

GTP-Binding Protein

Guanine Nucleotide Binding Protein

ADP-Ribosylation Factor

Related RAS Viral (r-ras) Oncogene

COMM Domain Containing

TIGAR

Mitochondrial Ribosomal Protein

Relaxin

Hairy and Enhancer of Split

Tissue Factor Pathway Inhibitor

Renin

Complement Component

Haptoglobin

TNF receptor-Associated Factor

Mitochondrial Transcription Factor

Reticulocalbin

Trafficking Protein Particle Complex

Heat Shock Protein

MOB1, Mps One Binder Kinase Activator

Retinoblastoma

Mortality Factor

Myelin Basic Protein

Retinoic Acid Early Transcript

Myelin Oligodendrocyte Glycoprotein

Transcription Elongation Factor

Myoglobin

Ag85

Retinoic Acid Receptor Responder

Albumin

Myosin Light Chain

Rho Family GTPase

Transferrin

Rho GDP Dissociation Inhibitor

Allergy

Ribosomal Protein

Transforming Growth Factor Beta Induced

Transgelin

Myxovirus

Translocase Of Outer Mitochondrial Membrane

NANOG

Troponin

NCK Adaptor Protein

Junctional Adhesion Molecule

Nescient Helix Loop Helix

NECTIN

Neuronal Calcium Sensor

Neutrophil Cytosolic Factor

NFKB Inhibitor

Ring Finger Protein

Triggering Receptor Expressed on Myeloid Cells

NHP2

Tripartite Motif

Alpha-2-HS-Glycoprotein

RNA Binding Motif Protein

Tropomyosin

Anaplasma

COP9 Signalosome

N-Myc Downstream Regulated

R-Spondin

Ankyrin Repeat Domain

C-Reactive Protein

TROVE Domain Family

Non-Metastatic Cells

RWD Domain Containing

Sclerostin

Hematological And Neurological Expressed

Angiogenin

Hemoglobin

Annexin

Trypsin

Secretagogin

Crystallin

Tubulin Folding Cofactor

Secreted Frizzled-Related Protein

NTF2-like Export Factor

Nucleobindin

Hemopexin

U6 Small Nuclear RNA

NPM

HNRNP

Nucleopurin

Secretoglobin

Nucleosome Assembly Protein

High-Mobility Group

Secretogranin

Tubulin Gamma

Orosomucoid

Selectin

Ubiquinol-Cytochrome C Reductase

Anterior Gradient Protein

Ubiquitin

ASF1 Anti-Silencing Function 1

HINT

C-type Lectin Domain

ATP Synthase Mitochondrial

Homeobox

Selenoprotein

ATPase

Septin

Serglycin

Homer Homolog

Serine Peptidase Inhibitor

Autophagy Related

Hypoxia-Inducible Factor

Serpin

Bartonella H.

Ig Heavy Chain Constant Region

CUE Domain Containing

B Cell Lymphoma

Cystatin

UCHL1

IMPAD1

UL16 binding protein

Inhibitor of DNA Binding

Uroplakin

Inhibitor of Growth Family

Integrin

Vacuolar Protein Sorting

Intercellular Adhesion Molecule

Vascular cell adhesion molecule

B9 Protein

SERTA Domain Containing

Babesia Microti

SH2 Domain

V-crk Sarcoma Virus CT10

SH3 Domain

Baculoviral IAP Repeat-Containing

Vimentin

Karyopherin

Visinin-Like Protein

BATF

Cysteine-Rich

Killer Cell

Basic Transcription Factor

MAF

SIGLEC

Cysteine-Rich Secretory Protein

Bax

V-ral Simian Leukemia Viral Oncogene

Beta 2 Microglobulin

Cytochrome

WAP Four-Disulfide Core Domain

Signal Recognition Particle

BID

Y. Enterocolitica

Signal Sequence Receptor

Biglycan

Signal-Regulatory Protein

Cytohesin

Bromodomain Containing

Zinc Finger

Cadherin

Cytokeratin

Single-Stranded DNA Binding Protein

Sirtuin

Bridging Integrator

SIX Homeobox

Calbindin

SLAM Family

SMAD

DCUN1D

DEAD Box Protein

Decorin

Density Lipoprotein

Developmental Pluripotency Associated

Dickkopf-Related Protein

DiGeorge Syndrome Critical Region

DNA-Damage Protein

Transmembrane Proteins

FC Receptor

Cancer Targets

Immune Checkpoint

CAR-T Cell Therapy Targets

Product List

LAGE3 Human

L Antigen Family Member 3 Human Recombinant

Recombinant human LAGE3, produced in E. coli, is a single polypeptide chain with 166 amino acids (residues 1-143) and a molecular weight of 17.2 kDa. A 23 amino acid His-tag is fused to the N-terminus of LAGE3, which is then purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT19519

Source

E.coli.

Appearance

A clear, sterile solution.

View Details

Lamin-A Human

Lamin-A Human Recombinant

Recombinant Human Lamin A, expressed in E. coli, is a single, non-glycosylated polypeptide chain composed of 645 amino acids with a molecular weight of 70 kDa. A 6xHis tag is fused to the N-terminus of the Lamin-A protein, which is purified using standard chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT19590

Source

Escherichia Coli.

Appearance

A clear, sterile-filtered solution.

View Details

SPECC1 Human

Sperm Antigen With Calponin Homology And Coiled-Coil 1 Human Recombinant

SPECC1 Human Recombinant, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 327 amino acids (458-761a.a). With a molecular mass of 37.7kDa, it features a 23 amino acid His-tag fused at the N-terminus. Purification is achieved through proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT19610

Source

Escherichia Coli.

Appearance

A clear and sterile solution.

View Details

LAMTOR2 Human

LAMTOR2 Human Recombinant

Recombinant human LAMTOR2, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 148 amino acids (residues 1-125) with a molecular weight of 15.9 kDa. The protein is fused to a 23-amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT19668

Source

Escherichia Coli.

Appearance

The product is a sterile, colorless solution.

View Details

SPG21 Human

Spastic Paraplegia 21 Human Recombinant

This product contains the SPG21 protein, which has been produced in E. coli bacteria. It is a single chain of 328 amino acids, with a molecular weight of 94.4 kDa. The protein is not glycosylated, meaning it does not have sugar molecules attached. A 20 amino acid His tag is present at the N-terminus for purification purposes. The protein has been purified using chromatography techniques.

Shipped with Ice Packs

Cat. No.

BT19677

Source

Escherichia Coli.

Appearance

Clear and colorless solution that has been sterilized by filtration.

View Details

LAMTOR4 Human

LAMTOR4 Human Recombinant

Recombinant LAMTOR4, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 122 amino acids (amino acids 1-99). It has a molecular weight of 13.1 kDa. The LAMTOR4 protein is fused to a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT19723

Source

Escherichia Coli.

Appearance

The product is a sterile, colorless solution.

View Details

SPI1 Human

Spi-1 Proto-Oncogene Human Recombinant

Recombinant human SPI1, expressed in E. coli, is a single polypeptide chain with a molecular weight of 33.6 kDa. It comprises 294 amino acids, with residues 1-271 corresponding to the SPI1 protein. A 23 amino acid His-tag is fused to the N-terminus to facilitate purification, which is achieved through proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT19782

Source

Escherichia Coli.

Appearance

A clear solution that has been sterilized through filtration.

View Details

LANCL1 Human

LanC Lantibiotic Synthetase Component C-Like 1 Human Recombinant

Recombinant human LANCL1, expressed in E. coli, is a non-glycosylated polypeptide chain. This single chain protein consists of 422 amino acids (1-399a.a), with a 23 amino acid His-tag attached to the N-terminus, resulting in a molecular weight of 47.7kDa. Purification is achieved using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT19798

Source

Escherichia Coli.

Appearance

Clear, colorless solution, sterile-filtered.

View Details

QKI Human

QKI Human Recombinant

Recombinant human QKI protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 364 amino acids (residues 1-341) and possessing a molecular weight of 40.1 kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT10276

Source

Escherichia Coli.

Appearance

A clear, sterile-filtered solution.

View Details

FSCN1 Human

Recombinant Human Fascin

Recombinant Human FSCN1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 513 amino acids (specifically, amino acids 1 through 493). It has a molecular weight of 56.7 kDa. A 20 amino acid His-Tag is fused to the N-terminus of the FSCN1. Purification is achieved using proprietary chromatographic methods.

Shipped with Ice Packs

Cat. No.

BT10339

Source

Escherichia Coli.

Appearance

The product is a colorless solution that has been sterilized through filtration.

View Details

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Introduction

Definition and Classification

The term “Other” can be defined in various contexts. In a general sense, it refers to something or someone that is different or distinct from the one already mentioned or known. In biological taxonomy, classification involves organizing living organisms into hierarchical categories based on their characteristics and evolutionary history .

Biological Properties

Biological properties of “Other” can be understood through key characteristics shared by living organisms, such as order, sensitivity or response to stimuli, reproduction, growth and development, regulation, homeostasis, and energy processing . These properties are expressed in various patterns and distributed across different tissues, contributing to the organism’s overall function and survival.

Biological Functions

The primary biological functions of “Other” include catalyzing chemical reactions, synthesizing and repairing DNA, transporting materials across cells, receiving and sending chemical signals, responding to stimuli, and providing structural support . These functions play crucial roles in immune responses and pathogen recognition, ensuring the organism’s defense mechanisms are active and effective.

Modes of Action

Modes of action describe the functional or anatomical changes resulting from exposure to a substance. This includes the interaction with other molecules and cells, binding partners, and downstream signaling cascades . For example, a mode of action could involve binding to DNA, leading to transcriptional regulation.

Regulatory Mechanisms

Regulatory mechanisms control the expression and activity of “Other” through transcriptional regulation and post-translational modifications . These mechanisms ensure that the biological processes are carried out efficiently and accurately, adapting to the organism’s needs and environmental changes.

Applications

In biomedical research, “Other” has various applications, including diagnostic tools and therapeutic strategies . For instance, understanding the biological properties and functions of different molecules can lead to the development of new treatments and diagnostic methods, improving healthcare outcomes.

Role in the Life Cycle

Throughout the life cycle, “Other” plays a significant role from development to aging and disease . This includes participating in growth, reproduction, and maintaining homeostasis. As organisms age, the efficiency of these processes may decline, leading to various age-related diseases.