Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

SBDS Human

Shwachman-Bodian-Diamond Syndrome Human Recombinant

This product consists of the recombinant human SBDS protein, expressed in E. coli and purified to a high degree. It is a single, non-glycosylated polypeptide chain comprising 270 amino acids (residues 1-250) with a molecular weight of 30.9 kDa. For purification purposes, a 20 amino acid His-tag is present at the N-terminus.
Shipped with Ice Packs
Cat. No.
BT14264
Source
Escherichia Coli.
Appearance
Clear, colorless and sterile-filtered solution.

HAPLN1 Human

Hyaluronan And Proteoglycan Link Protein 1 Human Recombinant

Recombinant HAPLN1, derived from human sources and produced in E.Coli, is a single, non-glycosylated polypeptide chain comprising 362 amino acids (specifically, residues 16-354). This protein exhibits a molecular weight of 40.9kDa. Notably, our HAPLN1 is engineered with a 23 amino acid His-tag at its N-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14302
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized through filtration.

HEBP1 Human

Heme Binding Protein 1 Human Recombinant

Recombinant HEBP1 Human is produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 212 amino acids (amino acids 1-189) with a molecular mass of 23.5 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.
BT14733
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile filtered solution.

HSCB Human

HscB Iron-Sulfur Cluster Co-Chaperone Human Recombinant

This recombinant HSCB protein, expressed in E. coli, is a single polypeptide chain consisting of 231 amino acids (residues 30-235). With a molecular weight of 26.7 kDa, it includes a 25 amino acid His-tag fused at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15305
Source
E.coli.
Appearance
The product is a sterile, colorless solution that has been filtered for purity.

HUS1 Human

HUS1 Checkpoint Homolog Human Recombinant

HUS1, a protein produced in E. coli, is a single polypeptide chain that lacks glycosylation. It consists of 300 amino acids (specifically, amino acids 1 to 280) and has a molecular weight of 33.8 kDa. A 20 amino acid His-tag is fused to the N-terminus of HUS1 to facilitate purification, which is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT15374
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized through filtration.

SET Human

SET Human Recombinant

Recombinant SET protein, of human origin, is produced in E. coli. It consists of a single polypeptide chain of 290 amino acids (residues 1-290) with a molecular weight of 35.9kDa. A 23 amino acid His-tag is fused to the N-terminus to facilitate purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15382
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

IBSP Human, HEK

Integrin Binding Sialoprotein Human Recombinant, HEK

Recombinant human IBSP protein, expressed in HEK293 cells, is a single glycosylated polypeptide chain. It consists of amino acids 17 to 317, totaling 307 amino acids, with a molecular weight of 34.3 kDa. The IBSP protein has a 6-amino acid His-tag fused at its C-terminus. Purification is achieved using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT15452
Source

HEK293 Cells.

Appearance
Clear, colorless solution that has been sterilized by filtration.

SHC1 Human

SHC-Transforming Protein 1 Human Recombinant

Recombinant human SHC1, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 494 amino acids (residues 1-474) with a molecular weight of 53.8 kDa. This protein includes a 20 amino acid His-Tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16229
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

SHFM1 Human

Split Hand/Foot Malformation Type 1 Human Recombinant

Recombinant human SHFM1, expressed in E. coli, is a non-glycosylated polypeptide chain containing 93 amino acids (amino acids 1-70) with a molecular weight of 10.7 kDa. Note that the molecular size observed on SDS-PAGE will be higher due to the presence of a 23 amino acid His-tag fused to the N-terminus. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16317
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

SIKE1 Human

Suppressor Of IKBKE 1 Human Recombinant

Recombinant human SIKE1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 230 amino acids (residues 1-207) and possessing a molecular weight of 26.1 kDa. A 23 amino acid His-tag is fused to the N-terminus of SIKE1. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16388
Source
Escherichia Coli.
Appearance
A clear solution that has undergone sterile filtration.
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 .

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