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

SMAC/DIABLO Human

SMAC/DIABLO Human Recombinant

Recombinant human Smac/Diablo, fused with an N-terminal T7-Tag, is produced in E. coli. This yields a single, non-glycosylated polypeptide chain comprising 199 amino acids, with a molecular weight of 22 kDa.

Shipped with Ice Packs

Cat. No.

BT17229

Source

Escherichia Coli.

Appearance

A clear, colorless solution that has been sterilized by filtration.

View Details

JMJD6 Human

Jumonji Domain Containing 6 Human Recombinant

Recombinant JMJD6 Human protein has been produced in E. coli. It is a single, non-glycosylated polypeptide chain consisting of 437 amino acids (1-414 a.a) with a molecular weight of 50.0kDa. The protein includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT17271

Source

Escherichia Coli.

Appearance

A clear, colorless solution that has been sterilized by filtration.

View Details

SMARCA4 Human

SMARCA4 Human Recombinant

Recombinantly produced in E. coli, SMARCA4 Human Recombinant is a single, non-glycosylated polypeptide chain comprising 211 amino acids (362-549aa) with a molecular weight of 25kDa. The protein is engineered with a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic methods.

Shipped with Ice Packs

Cat. No.

BT17289

Source

Escherichia Coli.

Appearance

A clear solution that has been sterilized by filtration.

View Details

JMJD7 Human

Jumonji Domain Containing 7 Human Recombinant

Recombinant human JMJD7, expressed in E. coli, is a non-glycosylated polypeptide chain. This single chain protein consists of 339 amino acids, with a truncated sequence spanning residues 1 to 316. It has a molecular weight of 38.3 kDa. The recombinant protein is further engineered to include a 23 amino acid His-tag at its N-terminus, facilitating purification using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT17353

Source

Escherichia Coli.

Appearance

The product is a clear solution that has been sterilized by filtration.

View Details

SNPH Human

Syntaphilin Human Recombinant

Recombinant Human SNPH, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 444 amino acids (1-424) with a molecular weight of 48.2 kDa. A 20 amino acid His-Tag is fused to the N-terminus. The protein undergoes purification using standard chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT17915

Source

Escherichia Coli.

Appearance

Clear, sterile-filtered solution.

View Details

SNTA1 Human

Syntrophin, Alpha 1 Human Recombinant

Recombinant human SNTA1, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 528 amino acids (1-505 a.a.). This protein has a molecular weight of 56.3 kDa and includes a 23 amino acid His-tag at the N-terminus. Purification is achieved using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT18024

Source

E.coli.

Appearance

A clear, colorless solution that has been sterilized by filtration.

View Details

SNUPN Human

Snurportin 1 Human Recombinant

Recombinant Human SNUPN, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 380 amino acids (specifically, residues 1-360) and exhibits a molecular weight of 43.3 kDa. A 20 amino acid His-Tag is fused to the N-terminus of SNUPN. Purification is achieved through proprietary chromatographic methods.

Shipped with Ice Packs

Cat. No.

BT18113

Source

Escherichia Coli.

Appearance

The product appears as a sterile, colorless solution after filtration.

View Details

ISOC2 Human

Isochorismatase Domain Containing 2 Human Recombinant

Recombinant human ISOC2, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 170 amino acids (59-205) with a molecular weight of 18 kDa. A 23 amino acid His-tag is fused to the N-terminus of ISOC2. Purification is carried out using proprietary chromatographic techniques.

Shipped with Ice Packs

Cat. No.

BT16923

Source

Escherichia Coli.

Appearance

Clear, colorless, and sterile filtered solution.

View Details

SLURP1 Human Dimer

Secreted LY6/PLAUR Domain Containing 1 Dimer Human Recombinant

Recombinant Human SLURP1, produced in E. coli, is a non-glycosylated homodimer with a structure encompassing residues Leu23 to Leu103. Each chain consists of 2x89 amino acids, including an 8 amino acid His tag located at the N-terminus. The calculated molecular mass for each chain is 9.9kDa.

Shipped with Ice Packs

Cat. No.

BT16980

Source

Escherichia Coli.

Appearance

White powder, lyophilized and filtered.

View Details

SLURP1 Human Monomer

Secreted LY6/PLAUR Domain Containing 1 Monomer Human Recombinant

Recombinant Human SLURP1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 89 amino acids, including an 8 aa His tag at the N-terminus, resulting in a calculated molecular mass of 9.9kDa. The sequence spans from Leu23 to Leu103.

Shipped with Ice Packs

Cat. No.

BT17146

Source

Escherichia Coli.

Appearance

White, lyophilized powder after 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.