Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

MINA Human

MYC Induced Nuclear Antigen Human Recombinant

Recombinant MINA protein, of human origin, has been produced in E. coli. It is a single, non-glycosylated polypeptide chain composed of 485 amino acids (specifically, amino acids 1 through 465) and has a molecular weight of 54.9 kDa. For purification purposes, a 20 amino acid His-tag has been added to the N-terminus of the MINA protein. The purification process involves the use of proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24434
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

TICAM2 Human

Toll-Like Receptor Adaptor Molecule 2 Human Recombinant

Recombinant human TICAM2, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 259 amino acids (residues 1-235). The protein exhibits a molecular weight of 29.4 kDa. For purification and detection purposes, a 24 amino acid His-tag is fused to the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24467
Source
E.coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

ANTXR2 Mouse

Anthrax Toxin Receptor 2 Mouse Recombinant

Produced in Sf9 insect cells, ANTXR2 is a single, glycosylated polypeptide chain with a molecular weight of 31.9 kDa. It consists of 295 amino acids (residues 32-318) and appears as a band at approximately 28-40 kDa on SDS-PAGE. This recombinant ANTXR2 protein is expressed with an 8-amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24484
Source
Sf9 Insect cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.

MIS12 Human

MIS12 Human Recombinant

Recombinant MIS12 Human protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 228 amino acids. This includes the 1-205 amino acids of MIS12 and an additional 23 amino acid His-tag at the N-terminus. The protein has a molecular weight of 26.5 kDa and is purified using proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT24497
Source
Escherichia Coli.
Appearance
The product appears as a clear solution after sterile filtration.

TIFA Human

TRAF-Interacting Protein with Forkhead-Associated Domain Human Recombinant

Recombinant Human TIFA, expressed in E.Coli, is a single, non-glycosylated polypeptide chain comprising 208 amino acids (specifically, amino acids 1 to 184). It possesses a molecular weight of 24kDa. To facilitate purification, a 24 amino acid His-tag is fused to the N-terminus of TIFA. The protein undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24533
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized through filtration.

AOC1 Human

Amine Oxidase Copper Containing 1 Human Recombinant

Recombinant human AOC1, expressed in HEK cells, is a single, glycosylated polypeptide chain with a molecular weight of 84.2 kDa. It encompasses amino acids 20 to 751, totaling 738 amino acids. The protein includes a 6-amino acid His-tag fused at the C-terminus to facilitate purification, which is achieved through proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT24555
Source

HEK293 Cells.

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

MLANA Human

Melan-A Human Recombinant

This product consists of a recombinant human MLANA protein produced in E. coli bacteria. The protein is a single chain of 94 amino acids (specifically, amino acids 48 to 118 of the full MLANA protein) and has a molecular weight of 10.4 kDa. For purification and detection purposes, a 23 amino acid His-tag is attached to the N-terminus of the protein. The protein has been purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT24564
Source
Escherichia Coli.
Appearance
The product is a clear solution that has been sterilized by filtration.

TIGIT Human

T-Cell Immunoreceptor With Ig And ITIM Domains Human Recombinant

This product consists of the extracellular domain of human TIGIT, specifically amino acids 22-141, fused to a 239 amino acid hlgG-His tag at the C-terminus. It is produced in Sf9 insect cells, resulting in a glycosylated polypeptide with a molecular weight of approximately 40 kDa. Due to glycosylation, the protein may appear larger (40-57 kDa) on SDS-PAGE. The protein has been purified using proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT24585
Source

Sf9, Baculovirus cells.

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

TIRAP Human

Toll-Interleukin 1 Receptor (TIR) Domain Containing Adaptor Protein Human Recombinant

Recombinant human TIRAP protein was expressed in E. coli and purified to a high degree. The protein encompasses amino acids 1-221 of the human TIRAP protein sequence, with an N-terminal Histidine tag (23 amino acids) for affinity purification. The molecular weight of the tagged protein is approximately 26.3 kDa.
Shipped with Ice Packs
Cat. No.
BT24992
Source
E.coli.
Appearance
Clear, colorless liquid, sterile filtered.

MOCS2 Human

Molybdenum Cofactor Synthesis 2 Human Recombinant

Recombinant human MOCS2 protein was produced in E. coli. It is a single polypeptide chain containing 224 amino acids (residues 1-188) with a molecular weight of 25.0 kDa. A 36 amino acid His-tag is present at the N-terminus. Purification was achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25000
Source
E.coli.
Appearance
A sterile, filtered, and colorless solution.
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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