BLNK Human

B-Cell Linker Human Recombinant
Cat. No.
BT27819
Source
Escherichia Coli.
Synonyms
B-cell linker protein, B-cell adapter containing a SH2 domain protein, B-cell adapter containing a Src homology 2 domain protein, Cytoplasmic adapter protein, Src homology 2 domain-containing leukocyte protein of 65 kDa, SLP-65, BLNK, BASH, SLP65, AGM4, LY57, BLNK-S, MGC111051.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

BLNK Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 476 amino acids (1-456 a.a.) and having a molecular mass of 52.6kDa (Molecular weight on SDS-PAGE will appear higher). The BLNK is purified by proprietary chromatographic techniques.

Product Specs

Introduction
BLNK, also known as B-cell linker, is a cytoplasmic adaptor protein crucial for B cell development. It plays a vital role in linking B cell receptor activation to downstream signaling pathways, influencing various cellular functions. Upon B cell receptor stimulation, BLNK interacts with effector proteins like GRB2, Vav, NCK, and PLC-g. Phosphorylation of BLNK by Syk tyrosine kinase facilitates the activation of these downstream effectors. Genetic mutations in the BLNK gene can lead to hypoglobulinemia and absent B cells, characterized by a developmental block in the pro- to pre-B-cell transition. BLNK protein deficiency is also observed in certain cases of pre-B acute lymphoblastic leukemia.
Description
Recombinant human BLNK protein is produced in E. coli with an N-terminal His tag (20 amino acids). This protein is a single, non-glycosylated polypeptide chain comprising 476 amino acids (residues 1-456) with a molecular weight of 52.6 kDa. Note that the protein may appear larger on SDS-PAGE due to the His tag. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The BLNK protein is provided as a 1 mg/ml solution in a buffer consisting of 20mM Tris-HCl (pH 8.0), 20% glycerol, 0.1M NaCl, 1mM DTT, and 0.1mM PMSF.
Stability
For short-term storage (up to 4 weeks), the BLNK solution can be stored at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Avoid repeated freezing and thawing cycles.
Purity
The purity of BLNK is greater than 90% as determined by SDS-PAGE analysis.
Synonyms
B-cell linker protein, B-cell adapter containing a SH2 domain protein, B-cell adapter containing a Src homology 2 domain protein, Cytoplasmic adapter protein, Src homology 2 domain-containing leukocyte protein of 65 kDa, SLP-65, BLNK, BASH, SLP65, AGM4, LY57, BLNK-S, MGC111051.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDKLNKITVP ASQKLRQLQK MVHDIKNNEG GIMNKIKKLK VKAPPSVPRR DYASESPADE EQQWSDDFDS DYENPDEHSD SEMYVMPAEE NADDSYEPPP VEQETRPVHP ALPFARGEYI DNRSSQRHSP PFSKTLPSKP SWPSEKARLT STLPALTALQ KPQVPPKPKG LLEDEADYVV PVEDNDENYI HPTESSSPPP EKAPMVNRST KPNSSTPASP PGTASGRNSG AWETKSPPPA APSPLPRAGK KPTTPLKTTP VASQQNASSV CEEKPIPAER HRGSSHRQEA VQSPVFPPAQ KQIHQKPIPL PRFTEGGNPT VDGPLPSFSS NSTISEQEAG VLCKPWYAGA CDRKSAEEAL HRSNKDGSFL IRKSSGHDSK QPYTLVVFFN KRVYNIPVRF IEATKQYALG RKKNGEEYFG SVAEIIRNHQ HSPLVLIDSQ NNTKDSTRLK YAVKVS.

Product Science Overview

Introduction

The B-cell linker (BLNK), also known as SLP-65, BASH, or BCA, is a crucial adaptor protein in B-cell receptor (BCR) signaling. It plays a significant role in the development and function of B cells, which are essential components of the adaptive immune system .

Structure and Localization

BLNK consists of several distinct domains:

  • N-terminal leucine zipper motif: This motif allows BLNK to localize to the plasma membrane through coiled-coil interactions with membrane proteins.
  • Acidic region: Following the leucine zipper motif, this region is rich in acidic amino acids.
  • Proline-rich region: This region is involved in protein-protein interactions.
  • C-terminal SH2 domain: This domain is crucial for binding phosphorylated tyrosine residues on other proteins .
Function

BLNK does not have intrinsic enzymatic activity. Instead, it functions as a scaffold protein, coordinating and regulating downstream signaling effectors in BCR signaling. This coordination is essential for B cell development, activation, and differentiation .

Role in BCR Signaling

Upon BCR engagement, BLNK is phosphorylated on tyrosine residues. This phosphorylation creates docking sites for various signaling molecules, including:

  • Syk kinase: Initiates the phosphorylation of BLNK.
  • Phospholipase Cγ2 (PLCγ2): Binds to phosphorylated BLNK and gets activated, leading to the production of second messengers.
  • Vav and Nck: These proteins are involved in cytoskeletal reorganization and cell adhesion .
Clinical Relevance

Mutations or deficiencies in BLNK can lead to immunodeficiencies and impaired B cell function. Understanding the role of BLNK in BCR signaling has implications for developing therapies for autoimmune diseases, immunodeficiencies, and B cell-related cancers .

Recombinant BLNK

Recombinant BLNK is produced using genetic engineering techniques, where the BLNK gene is cloned and expressed in suitable host cells. This recombinant protein is used in research to study BCR signaling pathways and to develop potential therapeutic interventions .

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