HSPB11 Human

Heat Shock Protein Family B Member 11 Human Recombinant
Cat. No.
BT18362
Source
Escherichia Coli.
Synonyms

Heat shock protein beta-11, Hspb11, Placental protein 25, PP25, C1orf41, HSPC034, IFT25.

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

HSPB11 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (1-144 a.a.) and having a molecular mass of 18.5kDa (Molecular weight on SDS-PAGE will appear higher).
HSPB11 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
HSPB11, a component of the IFT complex B, plays a role in placental development. The IFT complex B comprises IFT88, IFT57, TRAF3IP1, IFT52, IFT27, HSPB11, and IFT20.
Description
Produced in E. coli, this non-glycosylated HSPB11 protein is a single polypeptide chain with a molecular weight of 18.5 kDa (appears larger on SDS-PAGE). The 164 amino acid sequence includes amino acids 1-144 of the HSPB11 protein and a 20 amino acid His-tag fused at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
This solution contains 1 mg/ml of HSPB11 protein in a buffer of 20 mM Tris-HCl (pH 8.0), 10% glycerol, 2 mM DTT, and 0.1 M NaCl.
Stability
While HSPB11 Human Recombinant remains stable for up to 1 week at 4°C, it is recommended to store it below -18°C for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 90.0% using SDS-PAGE analysis.
Synonyms

Heat shock protein beta-11, Hspb11, Placental protein 25, PP25, C1orf41, HSPC034, IFT25.

Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MRKIDLCLSS EGSEVILATS SDEKHPPENI IDGNPETFWT TTGMFPQEFI ICFHKHVRIE RLVIQSYFVQ TLKIEKSTSK EPVDFEQWIE KDLVHTEGQL QNEEIVAHDG SATYLRFIIV SAFDHFASVH SVSAEGTVVS NLSS.

Product Science Overview

Gene and Protein Information
  • Gene Name: HSP90AB1
  • Aliases: HSPC2, HSPCB, HSP90-Beta, HSP84
  • Protein Class: Cancer-related genes, Plasma proteins, Transporters
  • Subcellular Location: Predominantly localized to the cytosol
Function and Mechanism

HSP90AB1 is a molecular chaperone that promotes the maturation, structural maintenance, and proper regulation of specific target proteins involved in cell cycle control and signal transduction. It undergoes a functional cycle linked to its ATPase activity, which likely induces conformational changes in client proteins, thereby causing their activation . The protein interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle, and chaperone function .

Expression and Localization

HSP90AB1 exhibits low tissue specificity and is expressed in various tissues, including the cerebral cortex, cerebellum, basal ganglia, hypothalamus, midbrain, amygdala, choroid plexus, hippocampal formation, spinal cord, retina, thyroid gland, parathyroid gland, adrenal gland, pituitary gland, lung, salivary gland, esophagus, tongue, stomach, duodenum, small intestine, colon, rectum, liver, gallbladder, pancreas, kidney, urinary bladder, testis, epididymis, seminal vesicle, prostate, vagina, ovary, fallopian tube, endometrium, cervix, placenta, breast, heart muscle, smooth muscle, skeletal muscle, adipose tissue, skin, appendix, spleen, lymph node, tonsil, bone marrow, and thymus .

Clinical Significance

HSP90AB1 is associated with various diseases, including larynx cancer and bronchitis . It is involved in critical pathways such as SARS-CoV-2 infection and inflammasomes . The protein’s role in gastric apoptosis and inflammation further underscores its importance in cellular homeostasis and disease mechanisms .

Research and Applications

Recombinant HSP90AB1 is widely used in research to study its function and interactions with other proteins. It serves as a model to understand the mechanisms of molecular chaperones and their role in maintaining cellular integrity under stress conditions.

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