HSPB8 Human

Heat Shock Protein 22 kDa Protein-8 Human Recombinant
Cat. No.
BT18710
Source
Escherichia Coli.
Synonyms
HSPB8, H11, HMN2, CMT2L, DHMN2, E2IG1, HMN2A, HSP22, Heat shock protein beta-8, Alpha-crystallin C chain, Small stress protein-like protein HSP22, E2-induced gene 1 protein, Protein kinase H11, CRYAC.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% 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.
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Description

Recombinant Human Heat Shock Protein 22 kDa Protein-8 is a full-length human HSP22 with an MW of 21604 Dalton produced in E.coli.

Product Specs

Introduction
HSPB8, also known as Heat Shock Protein 22 kDa Protein-8, exhibits chaperone activity that is influenced by temperature. While it has been proposed that HSPB8 functions as a manganese-dependent serine-threonine protein kinase, further research is needed to confirm this role. Mutations in the HSPB8 gene have been linked to distal hereditary motor neuropathy type II (DHMN2), a condition also referred to as distal spinal muscular atrophy (DSMA) or spinal muscular atrophy of the Charcot-Marie-Tooth type. DHMN2 is an autosomal dominant disorder primarily affecting lower motor neurons, leading to muscle weakness in the distal extremities.
Description
Recombinant Human Heat Shock Protein 22 kDa Protein-8 is a full-length protein derived from humans. It has a molecular weight of 21604 Daltons and is produced in E. coli.
Physical Appearance
White powder, sterile-filtered and lyophilized (freeze-dried).
Formulation
HSPB8 protein was lyophilized from a solution with a concentration of 1 mg/ml. The solution contained 20 mM Tris-acetate (pH 7.6), 10 mM NaCl, 0.1 mM EDTA, 0.1 mM PMSF, and 15 mM β-mercaptoethanol.
Solubility
To reconstitute the lyophilized HSPB8, it is recommended to dissolve it in sterile 18 MΩ-cm H2O at a concentration of at least 100 µg/ml. This solution can then be further diluted with other aqueous solutions.
Stability
Lyophilized HSPB8 remains stable at room temperature for up to three weeks. However, for long-term storage, it should be stored in a dry environment below -18°C. After reconstitution, HSPB8 should be stored at 4°C for 2 to 7 days. For extended storage, it is recommended to store it below -18°C. Adding a carrier protein (0.1% HSA or BSA) is also advised for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity of HSPB8 is determined by SDS-PAGE to be greater than 95.0%.
Synonyms
HSPB8, H11, HMN2, CMT2L, DHMN2, E2IG1, HMN2A, HSP22, Heat shock protein beta-8, Alpha-crystallin C chain, Small stress protein-like protein HSP22, E2-induced gene 1 protein, Protein kinase H11, CRYAC.
Source
Escherichia Coli.
Immunological Activity
Immunoreactivity is confirmed by reaction with monoclonal mouse antibodies against HSPB8.

Product Science Overview

Introduction

Heat Shock Protein 22 kDa Protein-8, also known as HSPB8 or HSP22, is a member of the small heat shock protein (sHSP) family. These proteins play a crucial role in protecting cells from stress by preventing the aggregation of misfolded proteins and assisting in their proper folding. HSPB8 is encoded by the HSPB8 gene in humans and is involved in various cellular processes, including protein homeostasis, signal transduction, and apoptosis.

Structure and Function

HSPB8 is a small heat shock protein with a molecular weight of approximately 22 kDa. It contains a conserved α-crystallin domain, which is characteristic of sHSPs and is essential for its chaperone activity. The protein functions as a molecular chaperone, binding to misfolded proteins and preventing their aggregation. This activity is particularly important under conditions of cellular stress, such as elevated temperatures, oxidative stress, and exposure to toxins .

Biological Roles

HSPB8 is involved in several critical biological processes:

  • Protein Homeostasis: HSPB8 helps maintain protein homeostasis by facilitating the proper folding of newly synthesized proteins and refolding or degrading damaged proteins.
  • Signal Transduction: HSPB8 participates in various signaling pathways, including those involved in stress responses and apoptosis.
  • Apoptosis: HSPB8 has been shown to play a role in regulating apoptosis, the programmed cell death process, by interacting with key apoptotic proteins.
  • Autophagy: HSPB8 is also involved in autophagy, a cellular process that degrades and recycles damaged organelles and proteins .
Expression and Tissue Distribution

HSPB8 is ubiquitously expressed in various tissues, with higher expression levels observed in tissues that are frequently exposed to stress, such as the heart, skeletal muscles, and the nervous system. Its expression can be induced by various stressors, including heat shock, oxidative stress, and inflammation .

Clinical Significance

Mutations in the HSPB8 gene have been associated with several neurodegenerative diseases, including Charcot-Marie-Tooth disease type 2L (CMT2L) and distal hereditary motor neuropathy type II (dHMNII). These conditions are characterized by progressive muscle weakness and atrophy, primarily affecting the distal muscles of the limbs .

Research and Therapeutic Potential

Due to its role in protein homeostasis and stress responses, HSPB8 is a potential therapeutic target for various diseases, including neurodegenerative disorders and cancer. Research is ongoing to develop small molecules and other therapeutic agents that can modulate the activity of HSPB8 and other heat shock proteins to treat these conditions .

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