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Description:

Epidermal Growth Factor Mouse Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-326

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Description

Epidermal Growth Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids including 3 intramolecular disulfide-bonds and having a molecular mass of 6 kDa.The EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The activity is determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells and is typically less than 0.1ng/ml.

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
NSYPGCPSSY DGYCLNGGVC MHIESLDSYT CNCVIGYSGD RCQTRDLRWW ELR.
Background
Exploring Novel Frontiers: Epidermal Growth Factor Mouse Recombinant and its Potential Therapeutic Implications
Abstract:
This research paper delves into the uncharted realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR), unraveling its intricate molecular attributes, cellular signaling, and therapeutic prospects. Employing state-of-the-art methodologies involving genetic engineering, in vitro assays, and animal models, this study uncovers the multifaceted responses elicited by EGF-MR. The findings underscore its promise as a versatile therapeutic agent, potentially revolutionizing regenerative medicine and cancer interventions.
Introduction:
Epidermal Growth Factor (EGF) plays a pivotal role in cellular dynamics. This paper ventures into the nuanced landscape of Epidermal Growth Factor Mouse Recombinant (EGF-MR), delving into its unique molecular characteristics and exploring the therapeutic horizons it presents.
Molecular Insights and Receptor Binding:
EGF-MR's interaction with the epidermal growth factor receptor (EGFR) sets the stage for intricate intracellular events. High-resolution structural analyses and binding kinetics studies elucidate the nuances of this interaction, revealing structural motifs that initiate downstream signaling cascades.
Cellular Signaling and Functional Responses:
EGF-MR initiates canonical and non-canonical signaling pathways, including the mitogen-activated protein kinase (MAPK) and phosphoinositide 3-kinase (PI3K)/Akt pathways. Through comprehensive phosphoproteomic analyses and live-cell imaging, the spatiotemporal dynamics of EGF-MR-induced responses come to light, showcasing its role in cell proliferation, migration, and anti-apoptotic effects.
Genetic Engineering and In Vitro Assays:
Precise genetic manipulation ensures optimal EGF-MR expression. Gene codon optimization and signal peptide selection are meticulously undertaken to facilitate efficient protein synthesis and secretion. In vitro assays, encompassing cell viability and wound healing studies, illuminate EGF-MR's impact on cellular behaviors.
In Vivo Implications and Therapeutic Prospects:
In animal models, EGF-MR emerges as a transformative factor in tissue regeneration. Customized wound healing assays unveil its potential in accelerating re-epithelialization and granulation tissue formation. Moreover, the modulation of tumor microenvironments suggests its applicability in cancer interventions.
Future Directions and Challenges:
While promising, challenges lie ahead, including understanding intricate cross-talk between signaling pathways. Future research should focus on refining delivery methods and optimizing dosing regimens to harness EGF-MR's full therapeutic potential.
Conclusion:
In a convergence of advanced methodologies and visionary therapeutic possibilities, Epidermal Growth Factor Mouse Recombinant takes center stage. Its distinctive molecular interactions and diverse cellular orchestration offer a glimpse into the future of regenerative medicine and targeted cancer therapies, propelling scientific progress into uncharted territories.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6 kDa.

What is the source or expression system of EGF Protein?
Escherichia Coli.

What is the Purity of EGF Protein?
EGF Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of EGF Protein?
The activity is determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells and is typically less than 0.1ng/ml.

What is the amino acid sequence of EGF Protein?
NSYPGCPSSY DGYCLNGGVC MHIESLDSYT CNCVIGYSGD RCQTRDLRWW ELR.
What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF Protein was purified using conventional chromatography techniques.

ProSpec'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.

Description:

Cathepsin-Z Human Recombinant, Sf9

Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.

Product # :

ENZ-1097

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Description

CTSZ produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 288 amino acids (24-303.a.) and having a molecular mass of 32.5kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).CTSZ is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CTSZ protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

The specific activity is determent as the ability of 1 unit to convert 1.0 pmole of Mca-PLGL-Dpa-AR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25C and is > 1,400 pmol/min/ug.

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Introduction
Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and a member of the peptidase C1 family. CTSZ, which is known also as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and as other members of this family, takes part in tumorigenesis.
Synonyms
Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
GLYFRRGQTC YRPLRGDGLA PLGRSTYPRP HEYLSPADLP KSWDWRNVDG VNYASITRNQ
HIPQYCGSCW AHASTSAMAD RINIKRKGAW PSTLLSVQNV IDCGNAGSCE GGNDLSVWDY
AHQHGIPDET CNNYQAKDQE CDKFNQCGTC NEFKECHAIR NYTLWRVGDY GSLSGREKMM
AEIYANGPIS CGIMATERLA NYTGGIYAEY QDTTYINHVV SVAGWGISDG TEYWIVRNSW
GEPWGERGWL RIVTSTYKDG KGARYNLAIE EHCTFGDPIV LEHHHHHH

ProSpec'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.

Description:

BolA Homolog 1 Human Recombinant

BolA-like protein 1, hBolA, BOLA1, CGI-143.

Product # :

PRO-302

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Description

BOLA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (21-137 a.a) and having a molecular mass of 14kDa.BOLA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BOLA1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
BolA Homolog 1(BOLA1) is a member of the bolA/yrbA family. BolA proteins, which include the: hBolA1, hBolA2, and hBolA3, are novel non-classical secreted proteins detected with bioinformatics and molecular biology experiments. The 3 BolA fusion proteins with c-Myc tag can be secreted into the culture medium of the transfected Cos-7 cells, even though they could not be colocalized with Golgi apparatus. Also, the secretion of 3 BolA proteins could not be inhibited after BFA treatment.
Synonyms
BolA-like protein 1, hBolA, BOLA1, CGI-143.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQGSAGSG AIGPVEAAIR TKLEEALSPE VLELRNESGG HAVPPGSETH FRVAVVSSRF EGLSPLQRHR LVHAALAEEL GGPVHALAIQ ARTPAQWREN SQLDTSPPCL GGNKKTLGTP.

ProSpec'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.

Description:

Complement Factor B Fragment a Human

Complement factor B (EC:3.4.21.47), C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, Complement factor B Ba fragment, Complement factor B Bb fragment, CFB, Complement Factor B, BFD, AHUS4, BF, BFD, CFAB, FB, FBI12, H2-Bf.

Product # :

PRO-2735

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Description

CFB-a Human produced in Human Plasma having a molecular mass of 33 kDa.

Source

Human Plasma.

Formulation

CFB-a solution (1mg/ml) contains Phosphate-buffered saline, pH 7.2.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Complement Factor B, also known as CFB, encodes complement factor B which is a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Once the alternative pathway is activated it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which connects with C3b to form the alternative pathway C3 convertase. Also, Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.
Synonyms
Complement factor B (EC:3.4.21.47), C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, Complement factor B Ba fragment, Complement factor B Bb fragment, CFB, Complement Factor B, BFD, AHUS4, BF, BFD, CFAB, FB, FBI12, H2-Bf.
Physical Appearance
Sterile filtered solution.
Stability
CFB-a Human is stable at 4°C if entire vial will be used within 2-4 weeks. Store, frozen below -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.

ProSpec'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.

Description:

Hypoxanthine-Guanine Phosphoribosyltransferase Clone PAT1D9AT, Mouse Anti Human

Hypoxanthine-Guanine Phosphoribosyltransferase , EC 2.4.2.8, HGPRT, HGPRTase, HPRT, HPRT1.

Product # :

ANT-727

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
HPRT1 has a main part in the generation of purine nucleotides through the purine salvage pathway. HPRT1 primarily functions to salvage purines from degraded DNA to renewed purine synthesis. Therefore, it performs as a catalyst in the reaction between guanine and phosphoribosyl pyrophosphate to form GMP.
Synonyms
Hypoxanthine-Guanine Phosphoribosyltransferase , EC 2.4.2.8, HGPRT, HGPRTase, HPRT, HPRT1.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human HPRT mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HPRT amino acids 1-218 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
Clone
PAT1D9AT.
Applications
HPRT antibody has been tested by ELISA, Western blot analysis, ICC/IF and Flow cytometry to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
HPRT antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

ProSpec'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.

Description:

Epidermal Growth Factor Rat

Urogastrone, URG, EGF.

Product # :

CYT-556

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Description

Epidermal Growth Factor Rat purified from submandibular gland is a single, glycosylated, polypeptide chain having a molecular mass of 6.15 kDa.The EGF is purified by proprietary chromatographic techniques.

Source

Adult Male Rat Submandibular Glands.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.01M sodium acetate buffer.

Purity

Greater than 99.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

More Info

Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Illuminating Epidermal Growth Factor Rat Recombinant: Deciphering Cellular Signaling and Therapeutic Potential
Abstract:
This research paper delves into the enigmatic realm of Epidermal Growth Factor Rat Recombinant (EGF-RR), unraveling its intricate molecular attributes, signaling cascades, and therapeutic prospects. By employing cutting-edge methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the multifaceted interplay between EGF-RR and cellular responses, offering novel avenues for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) is pivotal in cellular regulation. This paper navigates the complexities of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and potential therapeutic applications.
Protein Expression and Purification:
The study embarks on precise gene optimization to enhance EGF-RR expression. Purification techniques like affinity chromatography yield purified EGF-RR, primed for subsequent analyses.
Receptor Binding Assays and Ligand Interaction:
Employing advanced receptor binding assays, the paper deciphers EGF-RR's engagement with its cognate receptor. Quantitative assessments uncover binding kinetics, shedding light on the intricacies of EGF-RR's molecular interaction.
Cellular Signaling Pathways and Responses:
In vitro cellular assays unveil the signaling cascades ignited by EGF-RR. Through quantitative phosphoproteomic profiling, the study unravels phosphorylation events triggered by EGF-RR, delineating its role in cellular proliferation, migration, and differentiation.
Bioinformatics Insights and Structural Modeling:
Bioinformatics tools facilitate molecular dynamics simulations, offering insights into EGF-RR's receptor interactions and downstream signaling pathways. Structural modeling captures EGF-RR's conformational changes during signaling cascades.
Therapeutic Implications and Future Prospects:
EGF-RR's intricate signaling dynamics open avenues for therapeutic exploration. Harnessing its potential in wound healing, tissue regeneration, and cancer modulation emerges as a promising avenue for precision medicine.
Challenges and Future Directions:
Challenges, including context-specific responses, beckon further investigation. Future research should delve into cross-talk between signaling pathways and EGF-RR's contributions to diverse disease contexts.
Conclusion:
A fusion of advanced methodologies and visionary insights unveils Epidermal Growth Factor Rat Recombinant as an intriguing subject. Its molecular intricacies and complex cellular interplay ignite prospects for therapeutic breakthroughs, ushering in a new era of precision medicine.
What is the molecular weight/Mw of EGF RAT Protein?
EGF RAT Protein has a total Mw of 6.15kDa.

What is the source or expression system of EGF RAT Protein?
Adult Male Rat Submandibular Glands.

What is the Purity of EGF RAT Protein?
EGF RAT Protein is >99% pure as determined by SDS-PAGE.

What is the Biological Activity of EGF RAT Protein?
The biological functionality of EGF RAT Protein will be determined in the future.

What is the amino acid sequence of EGF RAT Protein?
EGF RAT Protein is composed from 53 amino acids.

What applications can EGF RAT Protein be used in?
EGF RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EGF RAT Protein?
The endotoxin level is minimal, EGF RAT Protein was purified using conventional chromatography techniques.

ProSpec'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.

Description:

Thyroid Stimulating Hormone Human Recombinant

Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.

Product # :

HOR-050

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Description

Thyroid Stimulating Hormone Human Recombinant produced in HEK 293 cells.

Source

HEK 293 cells.

Formulation

Lyophilized from a concentrated 50mM ammonium bicarbonate.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The protein is biologically active using Siemens Centaur CP is standardized against WHO 3rd IS 81/565.

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Synonyms
Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Recombinant TSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Recombinant TSH should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized recombinant TSH in sterile 10 mM Sodium Phosphate, 150 mM Sodium Chloride, 1 mg/ml BSA, 0.1% Sodium Azide (optional), pH 7.4.
Background
Thyroid-stimulating hormone (TSH), also known as thyrotropin, is a glycoprotein hormone produced by the anterior pituitary gland. Its primary function is to regulate thyroid gland activity by stimulating the synthesis and secretion of thyroid hormones, thyroxine (T4) and triiodothyronine (T3). Recombinant human TSH (rhTSH) has emerged as a valuable tool in clinical practice, particularly in the management of thyroid disorders and in diagnostic procedures involving the thyroid gland. This paper aims to provide an overview of research on rhTSH, including its mechanism of action, activity, and therapeutic applications.
The mechanism of action of rhTSH involves binding to the TSH receptor (TSHR) on the surface of thyroid follicular cells. This interaction activates intracellular signalling pathways, including cyclic adenosine monophosphate (cAMP) production and protein kinase A (PKA) activation. These pathways stimulate various cellular processes within thyroid follicular cells, such as iodine uptake, thyroid hormone synthesis, and secretion.
What is the source or expression system of TSH PROTEIN Protein?
HEK 293 cells.

What is the Purity of TSH PROTEIN Protein?
TSH PROTEIN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of TSH PROTEIN Protein?
The protein is biologically active using Siemens Centaur CP is standardized against WHO 3rd IS 81/565.

What applications can TSH PROTEIN Protein be used in?
TSH PROTEIN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for TSH PROTEIN Protein?
The endotoxin level is minimal, TSH PROTEIN Protein was purified using conventional chromatography techniques.

ProSpec'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.

Description:

Major Histocompatibility Complex Class II DR Beta 1 Human Recombinant, Sf9

DRB1, HLA DRB1, HLA-DR1B, HLA-DRB1, MHC class II antigen DRB1 16, DR-16, DR16, Human Leucocyte Antigen DRB1, MHC Class II HLA-DR-Beta Cell Surface Glycoprotein, MHC Class II HLA-DRw10-Beta.

Product # :

PRO-2553

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Description

HLA-DRB1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 207 amino acids (30-227a.a.) and having a molecular mass of 24.0kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). HLA-DRB1 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

HLA-DRB1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 30% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Major Histocompatibility Complex Class II DR Beta 1 also known as HLA-DRB1 ia a member of the HLA class II beta chain paralogs. Molecule class II is a heterodimer consisting of an alpha (DRA) and a beta chain (DRB), both anchored in the membrane. HLA-DRB1 takes an essential part in the immune system by presenting peptides derived from extracellular proteins. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). Furthermore, the beta chain is approximately 26- 28 kDa. It is encoded by 6 exons. While exon one encodes the leader peptide; exons 2 and 3 encode the two extracellular domains; exon 4 encodes the transmembrane domain; and exon 5 encodes the cytoplasmic tail.
Synonyms
DRB1, HLA DRB1, HLA-DR1B, HLA-DRB1, MHC class II antigen DRB1 16, DR-16, DR16, Human Leucocyte Antigen DRB1, MHC Class II HLA-DR-Beta Cell Surface Glycoprotein, MHC Class II HLA-DRw10-Beta.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPGDTRPRF LWQPKRECHF FNGTERVRFL DRYFYNQEES VRFDSDVGEF RAVTELGRPD AEYWNSQKDI LEQARAAVDT YCRHNYGVVE SFTVQRRVQP KVTVYPSKTQ PLQHHNLLVC SVSGFYPGSI EVRWFLNGQE EKAGMVSTGL IQNGDWTFQT LVMLETVPRS GEVYTCQVEH PSVTSPLTVE WRARSESAQS KHHHHHH

ProSpec'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.

Description:

Heat Shock Protein 90kDa Beta (GRP94) Member 1, Mouse Anti Human

ECGP, GP96, TRA1, GRP94, HSP90B1, Endoplasmin, Heat shock protein 90 kDa beta member 1, 94 kDa glucose-regulated protein, gp96 homolog, Tumor rejection antigen 1.

Product # :

ANT-325

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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
HSP90B1 is an abundant molecular chaperone resident endoplasmic reticulum (ER) lumenal stress protein which is part of the Hsp90 family. HSP90B1 is involved in maintaining protein homeostasis in the secretory pathway as well as functioning in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presentation cells. HSP90B1 has key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90B1 protein associates with numerous cochaperones and involved in folding of newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1 is highly expressed in human gastric carcinoma BGC-823 cells during the whole cell cycle.
Synonyms
ECGP, GP96, TRA1, GRP94, HSP90B1, Endoplasmin, Heat shock protein 90 kDa beta member 1, 94 kDa glucose-regulated protein, gp96 homolog, Tumor rejection antigen 1.
Physical Appearance
Sterile Filtered clear solution.
Immunogen
Anti-human HSP90B1 mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HSP90B1 amino acids 676-803 purified from E. coli.
Ig Subclass
Mouse IgG2a heavy chain and κ light chain.
Clone
P2H3AT.
Applications
HSP90B1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Immunofluorescence analysis is 1:100 ~ 1:200. Recommended starting dilution is 1:100.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
HSP90B1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

ProSpec'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.

Description:

Regenerating Islet-Derived 1 Beta Human Recombinant

Lithostathine-1-beta, Regenerating protein I beta, REG1B, REGL.

Product # :

PRO-391

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Description

The Recombinant Human REG 1 beta manufactured with N-terminal fusion of His Tag. The Human REG 1 beta His-Tagged Fusion Protein, produced in E. coli, is 17.8 kDa protein containing 144 amino acid residues of the Human REG 1 beta and 12 additional amino acid residues – His Tag (underlined).

Source

Escherichia Coli.

Formulation

Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 20mM Tris, pH 8.0.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Reg protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.
Reg I was found to be expressed mainly in pancreatic beta and acinoductular cells as well as gastric fundic enterochromaffin-like (ECL) cells. Reg I production in ECL cells is stimulated by gastrin, as well as by the proinflammatory cytokine, cytokine-induced neutrophil chemoattractant (CINC)-2Beta. In patients with chronic hypergastrinemia, Reg production is stimulated, with the increased proliferation of gastric mucosal cells. Patients with Helicobacter pylori infection also showed increased Reg production in the gastric mucosa, partly via increased plasma gastrin concentration and partly via increased proinflammatory cytokine production. The serum concentration of the reg-protein was significantly higher in patients with various pancreatic diseases than in normal controls, and was also significantly higher in patients with acute pancreatitis or chronic relapsing pancreatitis than in patients with chronic pancreatitis. Furthermore, the serum PSP/reg-protein concentration was also significantly increased in liver cirrhosis, choledocholithiasis, and various cancers of the digestive system.
Synonyms
Lithostathine-1-beta, Regenerating protein I beta, REG1B, REGL.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHAS HMQESQTELP NPRISCPEGT NAYRSYCYYF NEDPETWVDA DLYCQNMNSG NLVSVLTQAE GAFVASLIKE SSTDDSNVWI GLHDPKKNRR WHWSSGSLVS YKSWDTGSPS SANAGYCASL TSCSGFKKWK DESCEKKFSF VCKFKN.

ProSpec'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.

Description:

BAD Protein Human Recombinant

Bcl2 antagonist of cell death, BAD, Bcl-2-binding component 6, Bcl-XL/Bcl-2-associated death promoter, Bcl-2-like 8 protein, BAD Protein, BBC6, BCL2L8.

Product # :

PRO-458

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Description

Bcl2 antagonist of cell death (BAD) Human Recombinant full length protein expressed in E.coli, shows a 51 kDa band on SDS-PAGE(Icluding GST tag). The BAD protein is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BAD protein in 50mM Tris-Acetate, pH7.5, 1mM EDTA, 20% Glycerol.

More Info

Introduction
The Bcl-2 family of protein is characterized by its ability to modulate cell death under a broad range of physiologic conditions. Bcl-2 and several related proteins function to inhibit apoptosis while other members of the Bcl-2 family, such as Bax and Bak, enhance cell death under various conditions. Bad exhibits homology to Bcl-2 limited to the BH1, but not with Bax, Bcl-xS, Mcl-1, A1 or itself. In mammalian cells, Bad binds with greater affinity to Bcl-xL than to Bcl-2 and reverses the death repressor activity of Bcl-xL but not Bcl-2.
Synonyms
Bcl2 antagonist of cell death, BAD, Bcl-2-binding component 6, Bcl-XL/Bcl-2-associated death promoter, Bcl-2-like 8 protein, BAD Protein, BBC6, BCL2L8.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.
Applications
• ELISA
• Western Blotting.

ProSpec'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.

Description:

Septin-6 Human Recombinant

Septin 6, Septin 2, SEP2, KIAA0128, SEPT2.

Product # :

PRO-949

Price :

Quantity :

Shipping Method :

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Citations

Description

SEPT6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 457 amino acids (1-434) and having a molecular mass of 52.1 kDa.SEPT6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The SEPT6 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.1M NaCl and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
SEPT6 is a member of the septin family of GTPases and is functionally involved in cytokinesis and conservation of cellular morphology. SEPT6 interact with SEPT2. The genes encoding the mixed-lineage leukemia and SEPT2 breakpoint proteins are associated with one type of pediatric acute myeloid leukemia which is caused by reciprocal translocation between chromosomes 11 and X.
Synonyms
Septin 6, Septin 2, SEP2, KIAA0128, SEPT2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAATDIA RQVGEGCRTV PLAGHVGFDS LPDQLVNKSV SQGFCFNILC VGETGLGKST LMDTLFNTKF EGEPATHTQP GVQLQSNTYD LQESNVRLKL TIVSTVGFGD QINKEDSYKP IVEFIDAQFE AYLQEELKIR RVLHTYHDSR IHVCLYFIAP TGHSLKSLDL VTMKKLDSKV NIIPIIAKAD AISKSELTKF KIKITSELVS NGVQIYQFPT DDESVAEING TMNAHLPFAV IGSTEELKIG NKMMRARQYP WGTVQVENEA HCDFVKLREM LIRVNMEDLR EQTHTRHYEL YRRCKLEEMG FKDTDPDSKP FSLQETYEAK RNEFLGELQK KEEEMRQMFV QRVKEKEAEL KEAEKELHEK FDRLKKLHQD EKKKLEDKKK SLDDEVNAFK QRKTAAELPQ SQGSQAGGSQ TLKRDKEKKN NPWLCTE

ProSpec'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.

Description:

Acid Phosphatase Prostate, Human Recombinant, sf9

Acid Phosphatase, Prostate, Thiamine Monophosphatase, Ecto-5-Nucleotidase, 5-Nucleotidase, EC 3.1.3.2, TMPase, 5-NT, Prostatic Acid Phosphatase, Prostatic Acid Phosphotase, EC 3.1.3.5, ACP-3 , ACP3, PAP.

Product # :

ENZ-968

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Description

ACPP produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 360 amino acids (33-386 a.a.) and having a molecular mass of 41.8kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). ACPP is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

ACPP protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Acid phosphatase, prostate (ACPP) is a non-specific tyrosine phosphatase, which dephosphorylates a varied number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. ACPP has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma.
Synonyms
Acid Phosphatase, Prostate, Thiamine Monophosphatase, Ecto-5-Nucleotidase, 5-Nucleotidase, EC 3.1.3.2, TMPase, 5-NT, Prostatic Acid Phosphatase, Prostatic Acid Phosphotase, EC 3.1.3.5, ACP-3 , ACP3, PAP.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
KELKFVTLVF RHGDRSPIDT FPTDPIKESS WPQGFGQLTQ LGMEQHYELG EYIRKRYRKF LNESYKHEQV YIRSTDVDRT LMSAMTNLAA LFPPEGVSIW NPILLWQPIP VHTVPLSEDQ LLYLPFRNCP RFQELESETL KSEEFQKRLH PYKDFIATLG KLSGLHGQDL FGIWSKVYDP LYCESVHNFT LPSWATEDTM TKLRELSELS LLSLYGIHKQ KEKSRLQGGV LVNEILNHMK RATQIPSYKK LIMYSAHDTT VSGLQMALDV YNGLLPPYAS CHLTELYFEK GEYFVEMYYR NETQHEPYPL MLPGCSPSCP LERFAELVGP VIPQDWSTEC MTTNSHQGTE DSTDHHHHHH.

ProSpec'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.

Description:

Gliadin Alpha Wheat Recombinant

Product # :

PRO-2147

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Description

Recombinant Wheat Gliadin Alpha protein produced in E.Coli and fused to a 6 His Tag at C-terminus, having a theoretical Mw of 34557.64 Dalton, pI 7.70. Purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

Gliadin Alpha protein solution in 10mM Tris-HCl pH 7.2.

Purity

Protein is >90% pure.

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Introduction
Wheat Gliadin and related gluten components from barley, rye and possibly oats can cause an abnormal immune response called Celiac disease which is a chronic gastrointestinal disorder. Celiac disease characteristics are flattening of the jejunal mucosa and intestinal lesions of variable severity in hereditarily inclined individuals. Even though Celiac disease is not a classic autoimmune disease it is related to anti-tissue transglutaminase antibodies and gliadin antibodies tests are most recommended in screening populations at risk for CD and other gluten-sensitive enteropathies. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.
Physical Appearance
Sterile Filtered clear solution.
Stability
Gliadin Alpha although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
MVRVPVPQLQPQNPSQQQPQEQVPLVQQQQFPGQQQPFPPQQPYPQPQPFPSQQPYLQ
LQPFPQPQLPYPQPQLPYPQPQLPYPQPQPFRPQQPYPQSQPQYSQPQQPISQQQQQQQQ
QQQQKQQQQQQQQILQQILQQQLIPCRDVVLQQHSIAYGSSQVLQQSTYQLVQQLCCQQL
WQIPEQSRCQAIHNVVHAIILHQQQQQQQQQQQQPLSQVSFQQPQQQYPSGQGSFQPSQ
QNPQAQGSVQPQQLPQFEEIRNLALETLPAMCNVYIPPYCTIAPVGIFGTNYRHHHHHH.

ProSpec'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.

Description:

Ebola Zaire Recombinant Protein

Product # :

EVD-078

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Description

Nucleoprotein (NP) of Ebola virus has strong antigenicity in immune reactions. C-terminal of EBO-Z nucleoprotein was expressed and purified from E. coli, it migrated at 15kDa on SDS-PAGE and pI is 4.87. Ebola Zaire is fused to a c-terminal his tag and purified by a proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

Ebola Zaire protein solution is supplied in Phosphate buffer and 0.02% sodium azide.

Purity

>95% pure as determined by 12% SDS-PAGE (Coomassie blue stain).

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Introduction
Ebolavirus (EVD) belongs to the Filoviridae family of proteins which is comprised of a single-strand, non-infectious RNA genome. EVD genome is about 19,000 base pairs long and covers 7 genes in the order 3'-UTR-NP-VP35-VP40-GP-VP30-VP24-L-5'-UTR. There are 4 different ebolaviruses such as: Zaire (EBO-Z), Sudan (EBO-S), Cote d’Ivoire (EBO-CI) and Reston (EBO-R) that differ in amino acid sequence and location of where the gene overlaps. Similar to filoviruses and ebolavirions, EVD is a filamentous element that could appear in 3 forms: shepherd's crook, U shape or a 6 shape. Ebolaviruses may be coiled, toroid, or branched. Most ebolavirions are 80nm wideand 14,000nm long.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Applications
Immunoassay.

ProSpec'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.

Description:

Tyrosylprotein Sulfotransferase 2, sf9 Human Recombinant

Tyrosylprotein Sulfotransferase 2, EC 2.8.2.20, TPST-2, Transport And Golgi Organization 13 Homolog B (Drosophila), Transport And Golgi Organization 13 Homolog B, Protein-Tyrosine Sulfotransferase 2, Tyrosylprotein Phosphotransferase 2, Tyrosylprotein Sulfotransferase-2, TANGO13B.

Product # :

ENZ-949

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Quantity :

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Description

TPST2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 361 amino acids (26-377 a.a.) and having a molecular mass of 40.4kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). TPST2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TPST2 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Tyrosylprotein Sulfotransferase 2 (TPST2) is a member of the protein sulfotransferase family. TPST2 is a widely expressed protein, which catalyzes the O-sulfation of tyrosine residues within acidic regions of proteins. The TPST2 protein is a type II integral membrane protein located in the Golgi body.
Synonyms
Tyrosylprotein Sulfotransferase 2, EC 2.8.2.20, TPST-2, Transport And Golgi Organization 13 Homolog B (Drosophila), Transport And Golgi Organization 13 Homolog B, Protein-Tyrosine Sulfotransferase 2, Tyrosylprotein Phosphotransferase 2, Tyrosylprotein Sulfotransferase-2, TANGO13B.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPQQVLECR AVLAGLRSPR GAMRPEQEEL VMVGTNHVEY RYGKAMPLIF VGGVPRSGTT LMRAMLDAHP EVRCGEETRI IPRVLAMRQA WSKSGREKLR LDEAGVTDEV LDAAMQAFIL EVIAKHGEPA RVLCNKDPFT LKSSVYLSRL FPNSKFLLMV RDGRASVHSM ITRKVTIAGF DLSSYRDCLT KWNKAIEVMY AQCMEVGKEK CLPVYYEQLV LHPRRSLKLI LDFLGIAWSD AVLHHEDLIG KPGGVSLSKI ERSTDQVIKP VNLEALSKWT GHIPGDVVRD MAQIAPMLAQ LGYDPYANPP NYGNPDPFVI NNTQRVLKGD YKTPANLKGY FQVNQNSTSS HLGSSHHHHH H.

ProSpec'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.

Description:

Heat Shock Protein 90kDa Beta (GRP94) Member 1 Human Recombinant

ECGP, GP96, TRA1, GRP94, HSP90B1, Endoplasmin, Heat shock protein 90 kDa beta member 1, 94 kDa glucose-regulated protein, gp96 homolog, Tumor rejection antigen 1.

Product # :

HSP-091

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Description

HSP90B1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 819 amino acids (22-803 a.a.) and having a molecular mass of 94.4 kDa.HSP90B1 is expressed with a 36 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GRP94 protein solution (1mg/ml) contains 20mM Tris-HCl, pH-8, 1mM EDTA, 0.1M NaCl, 1mM DTT and 10% Glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
HSP90B1 is an abundant molecular chaperone resident endoplasmic reticulum (ER) lumenal stress protein which is part of the Hsp90 family. HSP90B1 is involved in maintaining protein homeostasis in the secretory pathway as well as functioning in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presentation cells. HSP90B1 has key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90B1 protein associates with numerous cochaperones and involved in folding of newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90B1 is highly expressed in human gastric carcinoma BGC-823 cells during the whole cell cycle.
Synonyms
ECGP, GP96, TRA1, GRP94, HSP90B1, Endoplasmin, Heat shock protein 90 kDa beta member 1, 94 kDa glucose-regulated protein, gp96 homolog, Tumor rejection antigen 1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMDDE VDVDGTVEED LGKSREGSRT DDEVVQREEE AIQLDGLNAS QIRELREKSE KFAFQAEVNR MMKLIINSLY KNKEIFLREL ISNASDALDK IRLISLTDEN ALSGNEELTV KIKCDKEKNL LHVTDTGVGM TREELVKNLG TIAKSGTSEF LNKMTEAQED GQSTSELIGQ FGVGFYSAFL VADKVIVTSK HNNDTQHIWE SDSNEFSVIA DPRGNTLGRG TTITLVLKEE ASDYLELDTI KNLVKKYSQF INFPIYVWSS KTETVEEPME EEEAAKEEKE ESDDEAAVEE EEEEKKPKTK KVEKTVWDWE LMNDIKPIWQ RPSKEVEEDE YKAFYKSFSK ESDDPMAYIH FTAEGEVTFK SILFVPTSAP RGLFDEYGSK KSDYIKLYVR RVFITDDFHD MMPKYLNFVK GVVDSDDLPL NVSRETLQQH KLLKVIRKKL VRKTLDMIKK IADDKYNDTF WKEFGTNIKL GVIEDHSNRT RLAKLLRFQS SHHPTDITSL DQYVERMKEK QDKIYFMAGS SRKEAESSPF VERLLKKGYE VIYLTEPVDE YCIQALPEFD GKRFQNVAKE GVKFDESEKT KESREAVEKE FEPLLNWMKD KALKDKIEKA VVSQRLTESP CALVASQYGW SGNMERIMKA QAYQTGKDIS TNYYASQKKT FEINPRHPLI RDMLRRIKED EDDKTVLDLA VVLFETATLR SGYLLPDTKA YGDRIERMLR LSLNIDPDAK VEEEPEEEPE ETAEDTTEDT EQDEDEEMDV GTDEEEETAK ESTAEKDEL.

ProSpec'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.

Description:

Serine/arginine-Rich Splicing Factor 1 Human Recombinant, Sf9

SRSF1, ASF, SF2, SF2p33, SFRS1, Splicing Factor, Arginine/Serine-Rich, 30-KD, A, Alternate Splicing Factor, SRp30a, ASF-1, Serine And Arginine Rich Splicing Factor 1, Pre-MRNA-Splicing Factor SF2, P33 Subunit, Splicing Factor, Arginine/Serine-Rich 1, Serine/Arginine-Rich Splicing Factor 1, Alternative-Splicing Factor 1, SR Splicing Factor 1, Splicing Factor 2.

Product # :

PRO-2417

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Description

SRSF1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 254 amino acids (1-248) and having a molecular mass of 28.5kDa. SRSF1 is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

SRSF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 100mM KCl, 1mM DTT, 0.2mM EDTA and 40% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Serine/arginine-rich splicing factor 1 (SFRS1) belongs to the arginine/serine-rich splicing factor protein family, and functions in both constitutive and alternative pre-mRNA splicing. SFRS1 binds to pre-mRNA transcripts and components of the spliceosome, and can either initiate or inhibit splicing depending on the position of the pre-mRNA binding site. The ability of SFRS1 to activate splicing is controlled by phosphorylation and interactions with other splicing factor associated proteins.
Synonyms
SRSF1, ASF, SF2, SF2p33, SFRS1, Splicing Factor, Arginine/Serine-Rich, 30-KD, A, Alternate Splicing Factor, SRp30a, ASF-1, Serine And Arginine Rich Splicing Factor 1, Pre-MRNA-Splicing Factor SF2, P33 Subunit, Splicing Factor, Arginine/Serine-Rich 1, Serine/Arginine-Rich Splicing Factor 1, Alternative-Splicing Factor 1, SR Splicing Factor 1, Splicing Factor 2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR RGGPPFAFVE FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG GGGGGGAPRG RYGPPSRRSE NRVVVSGLPP SGSWQDLKDH MREAGDVCYA DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF RSHEGETAYI RVKVDGPRSP SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR HSRSRSRTHH HHHH.

ProSpec'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.

Description:

Septin-3 Human Recombinant

Septin 3, SEP3, Neuronal-Specific Septin 3, Neuronal-Specific Septin-3, BK250D10.3, Neuronal-specific septin-3.

Product # :

PRO-2152

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Quantity :

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Description

SEPT3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-358 a.a) and having a molecular mass of 43.1kDa. SEPT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SEPT3 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Septin-3, also known as SEPT3 is a member of the septin family of GTPases. Members of this family are essential for cytokinesis. Furthermore, expression is up regulated by retinoic acid in a human teratocarcinoma cell line. The exact role of SEPT3 has not been determined yet. In addition, among its related pathways are Bacterial invasion of epithelial cells.
Synonyms
Septin 3, SEP3, Neuronal-Specific Septin 3, Neuronal-Specific Septin-3, BK250D10.3, Neuronal-specific septin-3.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSKGLPE TRTDAAMSEL VPEPRPKPAV PMKPMSINSN LLGYIGIDTI IEQMRKKTMK TGFDFNIMVV GQSGLGKSTL VNTLFKSQVS RKASSWNREE KIPKTVEIKA IGHVIEEGGV KMKLTVIDTP GFGDQINNEN CWEPIEKYIN EQYEKFLKEE VNIARKKRIP DTRVHCCLYF ISPTGHSLRP LDLEFMKHLS KVVNIIPVIA KADTMTLEEK SEFKQRVRKE LEVNGIEFYP QKEFDEDLED KTENDKIRQE SMPFAVVGSD KEYQVNGKRV LGRKTPWGII EVENLNHCEF ALLRDFVIRT HLQDLKEVTH NIHYETYRAK RLNDNGGLPP GEGLLGTVLP PVPATPCPTA E.

ProSpec'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.

Description:

Interleukin-9 Human Recombinant

P40, HP40, T-cell growth factor p40, IL-9, P40 cytokine.

Product # :

CYT-348

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
biological activity
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Description

Interleukin-9 Human Recombinant produced in E.Coli is a single, non-glycosylated single polypeptide chain containing 127 amino acids and having a molecular mass of 14,004 Dalton. The IL-9 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-9 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of human MO7e cells is less than 0.2 ng/ml, corresponding to a Specific Activity of >5.0×10⁶ IU/mg.

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Introduction
Factor that is thought to be a regulator of hematopoiesis. It has been shown to enhance the growth of human mast cells and megakaryoblastic leukemic cells as well as murine helper t-cell clones. IL-9 is a glycoprotein with a molecular weight of 32-39 that is derived from T-cells, and maps to human chromosome 5.
Synonyms
P40, HP40, T-cell growth factor p40, IL-9, P40 cytokine.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL9 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin-9 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQGCPTLAGI LDINFLINKM QEDPASKCHC SANVTSCLCL GIPSDNCTRP CFSERLSQMT NTTMQTRYPL IFSRVKKSVE VLKNNKCPYF SCEQPCNQTT AGNALTFLKS LLEIFQKEKM RGMRGKI.
Background
What is the molecular weight/Mw of IL9 HUMAN Protein?
IL9 HUMAN Protein has a total Mw of 14kDa.

What is the source or expression system of IL9 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL9 HUMAN Protein?
IL9 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL9 HUMAN Protein?
The ED50 as determined by the dose-dependent stimulation of human MO7e cells is less than 0.2 ng/ml, corresponding to a Specific Activity of >5.0×106 IU/mg.

What is the amino acid sequence of IL9 HUMAN Protein?
MQGCPTLAGI LDINFLINKM QEDPASKCHC SANVTSCLCL GIPSDNCTRP CFSERLSQMT NTTMQTRYPL IFSRVKKSVE VLKNNKCPYF SCEQPCNQTT AGNALTFLKS LLEIFQKEKM RGMRGKI.

What applications can IL9 HUMAN Protein be used in?
IL9 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL9 HUMAN Protein?
The endotoxin level is minimal, IL9 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL9 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL9 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec'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.

Description:

Tubby Like Protein 1 Human Recombinant

Tubby like protein 1, TUBL1, RP14, LCA15, tubby-related protein 1.

Product # :

PRO-1191

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Shipped with Ice Packs

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Description

TULP1 Human Recombinant produced in E. coli is a single polypeptide chain containing 276 amino acids (290-542) and having a molecular mass of 31.1 kDa.TULP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TULP1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Tubby-related protein 1 (TULP1) belongs to the TULP family of 4 proteins (TUB and TULP1, -2, and -3), categorized structurally by the highly conserved C-terminal half of the protein. Tubby-like gene family (TULPs) members are found in plants, vertebrates, and invertebrates and encode proteins of unknown function. TULP proteins share a conserved C-terminal region of roughly 200 amino acid residues. In the retina, TULP1 is observed exclusively in the photoreceptor cells, localizing predominantly in the inner segments and connecting cilium and to a lesser degree in the perinuclear cytoplasm and synaptic termini. TULP1 gene mutations are linked with retinitis pigmentosa.
Synonyms
Tubby like protein 1, TUBL1, RP14, LCA15, tubby-related protein 1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEPREFVL RPAPQGRTVR CRLTRDKKGM DRGMYPSYFL HLDTEKKVFL LAGRKRKRSK TANYLISIDP TNLSRGGENF IGKLRSNLLG NRFTVFDNGQ NPQRGYSTNV ASLRQELAAV IYETNVLGFR GPRRMTVIIP GMSAENERVP IRPRNASDGL LVRWQNKTLE SLIELHNKPP VWNDDSGSYT LNFQGRVTQA SVKNFQIVHA DDPDYIVLQF GRVAEDAFTL DYRYPLCALQ AFAIALSSFD GKLACE

ProSpec'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.

Description:

Interleukin-1 Receptor Like-1 Human Recombinant, Sf9 Active

Interleukin 1 Receptor Like 1, Homolog Of Mouse Growth Stimulation-Expressed, DER4, ST2, T1, Interleukin 1 Receptor-Related Protein, Interleukin-1 Receptor-Like 1, Growth Stimulation-Expressed, Protein ST2, FIT-1, IL33R, ST2L, ST2V, Interleukin-1 receptor-like 1.

Product # :

CYT-1052

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Shipped with Ice Packs

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SDS-PAGE
Citations

Description

IL1RL1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 318 amino acids (19-328a.a.) and having a molecular mass of 36.0kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IL1RL1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL1RL1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to inhibit proliferation using D10.G4.1 mouse helper T cells. The ED50 for this effect is less or equal to 10ng/ml with IL-33.

SDS-PAGE

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Introduction
The IL1RL1 gene is a member of the IL-1 receptor family, encoding a transmembrane protein with a structure similar to IL-1R1. IL1RL1 is a receptor for interleukin-33, its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. IL1RL1 may possibly be involved in helper T-cell function. IL1RL1 is highly expressed in kidney, lung, placenta, stomach, skeletal muscle, colon and small intestine.A soluble form of the IL1RL1 is produced from the same gene by alternative splicing and was shown to be expressed in several cell types including fibroblasts and mast cells. Soluble IL1RL1 also acts as a negative regulator of Th2 cytokine production and high levels have been reported in several disease states and conditions including asthma, sepsis and myocardial infarction.Analysis of the similar gene in mouse suggested that the IL1RL1 receptor can be induced by proinflammatory stimuli, and may be involved in the function of helper T cells.
Synonyms
Interleukin 1 Receptor Like 1, Homolog Of Mouse Growth Stimulation-Expressed, DER4, ST2, T1, Interleukin 1 Receptor-Related Protein, Interleukin-1 Receptor-Like 1, Growth Stimulation-Expressed, Protein ST2, FIT-1, IL33R, ST2L, ST2V, Interleukin-1 receptor-like 1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
KFSKQSWGLE NEALIVRCPR QGKPSYTVDW YYSQTNKSIP TQERNRVFAS GQLLKFLPAA VADSGIYTCI VRSPTFNRTG YANVTIYKKQ SDCNVPDYLM YSTVSGSEKN SKIYCPTIDL YNWTAPLEWF KNCQALQGSR YRAHKSFLVI DNVMTEDAGD YTCKFIHNEN GANYSVTATR SFTVKDEQGF SLFPVIGAPA QNEIKEVEIG KNANLTCSAC FGKGTQFLAA VLWQLNGTKI TDFGEPRIQQ EEGQNQSFSN GLACLDMVLR IADVKEEDLL LQYDCLALNL HGLRRHTVRL SRKNPIDHHS LEHHHHHH.
Background
What is the molecular weight/Mw of IL1RL1 HUMAN, SF9 ACTIVE Protein?
IL1RL1 HUMAN, SF9 ACTIVE Protein has a total Mw of 36kDa.

What is the source or expression system of IL1RL1 HUMAN, SF9 ACTIVE Protein?
Sf9, Baculovirus cells.

What is the Purity of IL1RL1 HUMAN, SF9 ACTIVE Protein?
IL1RL1 HUMAN, SF9 ACTIVE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1RL1 HUMAN, SF9 ACTIVE Protein?
Measured by its ability to inhibit proliferation using D10.G4.1 mouse helper T cells. The ED50 for this effect is less or equal to 10ng/ml with IL-33.

What is the amino acid sequence of IL1RL1 HUMAN, SF9 ACTIVE Protein?
KFSKQSWGLE NEALIVRCPR QGKPSYTVDW YYSQTNKSIP TQERNRVFAS GQLLKFLPAA VADSGIYTCI VRSPTFNRTG YANVTIYKKQ SDCNVPDYLM YSTVSGSEKN SKIYCPTIDL YNWTAPLEWF KNCQALQGSR YRAHKSFLVI DNVMTEDAGD YTCKFIHNEN GANYSVTATR SFTVKDEQGF SLFPVIGAPA QNEIKEVEIG KNANLTCSAC FGKGTQFLAA VLWQLNGTKI TDFGEPRIQQ EEGQNQSFSN GLACLDMVLR IADVKEEDLL LQYDCLALNL HGLRRHTVRL SRKNPIDHHS LEHHHHHH.

What applications can IL1RL1 HUMAN, SF9 ACTIVE Protein be used in?
IL1RL1 HUMAN, SF9 ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1RL1 HUMAN, SF9 ACTIVE Protein?
The endotoxin level is minimal, IL1RL1 HUMAN, SF9 ACTIVE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL1RL1 HUMAN, SF9 ACTIVE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL1RL1 HUMAN, SF9 ACTIVE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec'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.

Description:

Chitinase Clostridium Paraputrificum Recombinant

Product # :

ENZ-031

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Chitinase Clostridium Paraputrificum Recombinant fused with a His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 582 amino acids and having a molecular mass of 64.2kDa. The Chitinase is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Chitinase lyophilized from a 0.2µm filtered concentrated solution in PBS.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Chitinase is a digestive enzyme which breaks down glycosidic bonds in chitin. Due to chitin being a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods), chitinases are usually found in organisms that either need to remake their own chitin or to dissolve and digest the chitin of fungi or animals. Chitinivorous organisms include many bacteria genuses such as Aeromonas, Bacillus, Vibrio, among others, which may be pathogenic or detritivorous. Chitinase expression is mediated by the NPR1 gene and the salicylic acid pathway, both of which are involved in resisting fungal and insect attack. Human chitinases appear in gastric juices. They are likely to be digestive chitinases, for catabolic activity. Chitinase activity is identified systemically in humans, in the blood, and possibly cartilage. Chitinase has been related to allergies, asthma in particular has been linked to enhanced chitinase expression levels, also dust mites and mold spores which are both chitin covered.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Chitinase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Chitinase should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Chitinase in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MRGSGSHHHH HHMYYGDWSI WGGQGNFYPK DIPADKLTHL NFAFMDFNSS GELIYCDKDA AIGHPLGNLG VTYGDVNGGI LNAFQVLKSE NPNLKIGVSL GGWSKSGDFS TIAATPSIRA KFVENVMKFI KYTNMDFVDI DWEYPGDYRE PDKTDNINDE GTPNASAGDK ENYILLLQDL KEALNKQGKE LGKVYELSVA LPAGVSKIEK GIDVDKLFNI VDFANIMTYD MAGAWSTTSG HQTALYTNPN APEEYKGLSV DESVKYYISQ GAEREKIVVG AAYYTRGWEQ VSDKGTDPNN PGLFGEAAVV NKDADLSPTP GALNEAPMKN GEGGRAGGVW GYNALDKLKS KYTGLKEYWD DSAKAPYLYN SETGAFFTYD NIRSIQEKAK YVKENNLGGI IGWMASQDAT TNSTKRDELT TATKESLFGK EDLPKYEIKY TENDITCTVT PVKQSWGSGG VLKMSITNNE KLDESGEVLS TVETSAKTVK NMKVYIKTDG IAITGSQYPA GPVTKEGDYY VIDFGKISDG KLMKAGITFT FDLNLDKAIE DTNNIISIEV SQRMYQTSPE FNRQTIWENT NS.

ProSpec'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.

Description:

Glial Fibrillary Acidic Protein Bovine

Glial fibrillary acidic protein, GFAP.

Product # :

PRO-2784

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

GFAP Bovine having a calculated molecular mass of 52 kDa, pI-5.4.

Source

Bovine spinal cord.

Formulation

GFAP was lyophilized from a 1mg/ml solution containing 10mM sodium phosphate buffer pH 7.5, 6M urea, 1mM EDTA, 2mM DTT and 10mM methylammonium chloride.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Synonyms
Glial fibrillary acidic protein, GFAP.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Store the lyophilized GFAP between 2-8°C, do not freeze. Upon reconstitution GFAP should be stored at -20°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GFAP in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Glial fibrillary acidic protein (GFAP) is a key intermediate filament protein found predominantly in astrocytes, a type of glial cell in the central nervous system. While extensive research has been conducted on GFAP in rodents and humans, the study of GFAP in bovine brain tissue is an emerging area with potential for advancing our understanding of astrocytic function and neurological health in larger mammals. Bovine brains provide a unique model system due to their size and complexity, making them valuable for investigating astrocyte-specific functions. This research aims to provide a comprehensive exploration of GFAP in bovine brain tissue, shedding light on its functions and implications for neurological health.
The primary objective of this research is to elucidate the role of GFAP in bovine brain tissue, particularly in astrocyte structure and function. In vitro and ex vivo experiments, utilizing bovine astrocyte cultures and brain tissue slices, will be conducted to investigate how GFAP contributes to astrocytic morphology, intracellular signaling, and response to neuronal injury or disease. Understanding these mechanisms is fundamental for deciphering the complexities of astrocyte biology in large mammalian brains.
The second objective is to assess the relevance of bovine GFAP in neurodegenerative diseases and brain injuries. Studies involving bovine brain models of neurodegenerative conditions such as Alzheimer's disease or traumatic brain injury will be conducted to evaluate the role of GFAP in disease progression, neuroinflammation, and tissue repair. These investigations may provide valuable insights into potential therapeutic strategies for neurological disorders.
The third objective is to explore the potential applications of bovine GFAP in biotechnology and medical research. Research will investigate the use of bovine astrocyte cultures as models for studying astrocyte-neuron interactions and for developing tissue engineering approaches for neurological repair and regeneration.
By delving into the functions and roles of GFAP in bovine brain tissue, this research aims to expand our knowledge of astrocyte biology, its implications for neurological health, and its potential applications in biotechnology and medical research.

ProSpec'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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