Search: 1000 results found for "Tumor Necrosis Factor"

Description:

Vitronectin Human Recombinant

Vitronectin precursor, V75, VN, VNT, Vitronectin, VTN, S-protein, Serum-spreading factor, Vitronectin V65 subunit, Vitronectin V10 subunit, Somatomedin-B.

Product # :

PRO-2008

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Description

VTN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 482 amino acids (20-478 a.a) and having a molecular mass of 54.7kDa. VTN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

VTN protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Vitronectin (VTN) which is a part of the pexin family is a cell adhesion and spreading factor found in serum and tissues. VTN interacts with glycosaminoglycans and proteoglycans. VTN inhibits the membrane-damaging effect of the terminal cytolytic complement pathway and binds to numerous serpin serine protease inhibitors. Scientists have been noticed an over expression of VTN, integrins and plasminogen in migrating cells during wound healing.
Synonyms
Vitronectin precursor, V75, VN, VNT, Vitronectin, VTN, S-protein, Serum-spreading factor, Vitronectin V65 subunit, Vitronectin V10 subunit, Somatomedin-B.
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 MGSDQESCKG RCTEGFNVDK KCQCDELCSY YQSCCTDYTA ECKPQVTRGD VFTMPEDEYT VYDDGEEKNN ATVHEQVGGP SLTSDLQAQS KGNPEQTPVL KPEEEAPAPE VGASKPEGID SRPETLHPGR PQPPAEEELC SGKPFDAFTD LKNGSLFAFR GQYCYELDEK AVRPGYPKLI RDVWGIEGPI DAAFTRINCQ GKTYLFKGSQ YWRFEDGVLD PDYPRNISDG FDGIPDNVDA ALALPAHSYS GRERVYFFKG KQYWEYQFQH QPSQEECEGS SLSAVFEHFA MMQRDSWEDI FELLFWGRTS AGTRQPQFIS RDWHGVPGQV DAAMAGRIYI SGMAPRPSLA KKQRFRHRNR KGYRSQRGHS RGRNQNSRRP SRATWLSLFS SEESNLGANN YDDYRMDWLV PATCEPIQSV FFFSGDKYYR VNLRTRRVDT VDPPYPRSIA QYWLGCPAPG HL.

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:

RAN Guanine Nucleotide Release Factor Human Recombinant

Ran guanine nucleotide release factor, RanGNRF, Ran-binding protein MOG1, RANGRF, MOG1, HSPC165, HSPC236, MDS5.

Product # :

PRO-1149

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Description

RANGRF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-186 a.a) and having a molecular mass of 23kDa.RANGRF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

RANGRF protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
RANGRF is a protein which acts as a guanine nucleotide release factor in mouse and regulates the expression and function of the Nav1.5 cardiac sodium channel in human. RANGRF also controls the intracellular trafficking of RAN. In cardiac cells, the RANGRF appears to regulate the cell surface localization of SCN5A.
Synonyms
Ran guanine nucleotide release factor, RanGNRF, Ran-binding protein MOG1, RANGRF, MOG1, HSPC165, HSPC236, MDS5.
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 MGSHMEPTRD CPLFGGAFSA ILPMGAIDVS DLRPVPDNQE VFCHPVTDQS LIVELLELQA HVRGEAAARY HFEDVGGVQG ARAVHVESVQ PLSLENLALR GRCQEAWVLS GKQQIAKENQ QVAKDVTLHQ ALLRLPQYQT DLLLTFNQPP PDNRSSLGPE NLSPAPWSLG DFEQLVTSLT LHDPNIFGPQ.

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:

SIL1 Human Recombinant

SIL1 homolog endoplasmic reticulum chaperone (S. cerevisiae), nucleotide exchange factor SIL1, Marinesco-Sjogren syndrome, BiP-associated protein, ULG5, MSS, BAP.

Product # :

PRO-1187

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Description

SIL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 439 amino acids (32-461) and having a molecular mass of 50.0 kDa.SIL1 is fused to a 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The SIL1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
SIL1 is localized to endoplasmic reticulum (ER). SIL1 is an N-linked glycoprotein with an N-terminal ER targeting sequence, 2 putative N-glycosylation sites, and a C-terminal ER retention signal. SIL1 acts as a nucleotide exchange factor for another unfolded protein response protein. Mutations in SIL1 are linked to Marinesco-Sjogren syndrome.
Synonyms
SIL1 homolog endoplasmic reticulum chaperone (S. cerevisiae), nucleotide exchange factor SIL1, Marinesco-Sjogren syndrome, BiP-associated protein, ULG5, MSS, BAP.
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
MHQNLKEFAL TNPEKSSTKE TERKETKAEE ELDAEVLEVF HPTHEWQALQ PGQAVPAGSH VRLNLQTGER EAKLQYEDKF RNNLKGKRLD INTNTYTSQD LKSALAKFKE GAEMESSKED KARQAEVKRL FRPIEELKKD FDELNVVIET DMQIMVRLIN KFNSSSSSLE EKIAALFDLE YYVHQMDNAQ DLLSFGGLQV VINGLNSTEP LVKEYAAFVL GAAFSSNPKV QVEAIEGGAL QKLLVILATE QPLTAKKKVL FALCSLLRHF PYAQRQFLKL GGLQVLRTLV QEKGTEVLAV RVVTLLYDLV TEKMFAEEEA ELTQEMSPEK LQQYRQVHLL PGLWEQGWCE ITAHLLALPE HDAREKVLQT LGVLLTTCRD RYRQDPQLGR TLASLQAEYQ VLASLELQDG EDEGYFQELL GSVNSLLKEL RLEHHHHHH.

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:

Stromal Cell Derived Factor-1 Beta Human Recombinant (CXCL12)

SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b.

Product # :

CHM-325

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Shipped at Room temp

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Description

Stromal Cell-Derived Factor-1 beta Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 72 amino acids and having a molecular mass of 8508 Dalton. The SDF-1b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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 specific activity as determined by its ability to chemoattract human peripheral T cells activated with PHA and IL-2 using a concentation of 20-80ng/ml corresponding to a Specific Activity of 12,500-50,000IU/mg.

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Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SDF-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 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 Stromal Cell-Derived Factor-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNKRF KM.
Background
What is the molecular weight/Mw of CXCL12 HUMAN BETA Protein?
CXCL12 HUMAN BETA Protein has a total Mw of 8.5kDa.

What is the source or expression system of CXCL12 HUMAN BETA Protein?
Escherichia Coli.

What is the Purity of CXCL12 HUMAN BETA Protein?
CXCL12 HUMAN BETA Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL12 HUMAN BETA Protein?
The specific activity as determined by its ability to chemoattract human peripheral T cells activated with PHA and IL-2 using a concentation of 20-80ng/ml corresponding to a Specific Activity of 12,500-50,000IU/mg.

What is the amino acid sequence of CXCL12 HUMAN BETA Protein?
KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNKRF KM.

What applications can CXCL12 HUMAN BETA Protein be used in?
CXCL12 HUMAN BETA Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL12 HUMAN BETA Protein?
The endotoxin level is minimal, CXCL12 HUMAN BETA Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL12 HUMAN BETA 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 CXCL12 HUMAN BETA?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
Protein content
Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm using the absorbency value of 1.06 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of SDF-1b as a Reference Standard.

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:

GRO/KC (CXCL1) Mouse Recombinant, His Tag

Growth-regulated alpha protein, CXCL1, Platelet-derived growth factor-inducible protein KC, Secretory protein N51, KC, Fsp, N51, gro, Gro1, Mgsa, Scyb1, chemokine (C-X-C motif) ligand 1.

Product # :

CHM-002

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Description

GRO1/KC Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 97 amino acids (25-96 a.a.) and having a molecular mass of 10.5kDa.GRO1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GRO1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophils and epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.
Synonyms
Growth-regulated alpha protein, CXCL1, Platelet-derived growth factor-inducible protein KC, Secretory protein N51, KC, Fsp, N51, gro, Gro1, Mgsa, Scyb1, chemokine (C-X-C motif) ligand 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 MGSHMAPIAN ELRCQCLQTM AGIHLKNIQS LKVLPSGPHC TQTEVIATLK NGREACLDPE APLVQKIVQK MLKGVPK.
Background
What is the molecular weight/Mw of CXCL1 MOUSE, HIS Protein?
CXCL1 MOUSE, HIS Protein has a total Mw of 10.5kDa.

What is the source or expression system of CXCL1 MOUSE, HIS Protein?
Escherichia Coli.

What is the Purity of CXCL1 MOUSE, HIS Protein?
CXCL1 MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL1 MOUSE, HIS Protein?
The biological functionality of CXCL1 MOUSE, HIS Protein will be determined in the future.

What is the amino acid sequence of CXCL1 MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMAPIAN ELRCQCLQTM AGIHLKNIQS LKVLPSGPHC TQTEVIATLK NGREACLDPE APLVQKIVQK MLKGVPK.

What applications can CXCL1 MOUSE, HIS Protein be used in?
CXCL1 MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL1 MOUSE, HIS Protein?
The endotoxin level is minimal, CXCL1 MOUSE, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL1 MOUSE, HIS 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 CXCL1 MOUSE, HIS?
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:

Bone Morphogenetic protein Receptor-1B Human Recombinant

Bone Morphogenetic Protein Receptor, Type IB, BMP Type-1B Receptor, EC 2.7.11.30, BMPR-1B, ALK6, Bone Morphogenetic Protein Receptor Type-1B, Serine/Threonine Receptor Kinase, CDw293 Antigen, EC 2.7.11, CDw293, ALK-6, Bone morphogenetic protein receptor type-1B.

Product # :

CYT-897

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Description

BMPR1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (14-126 a.a) and having a molecular mass of 15.1kDa. BMPR1B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BMPR1B protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol, 1mM DTT and 0.1mM PMSF.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Bone Morphogenetic protein Receptor-1B, also known as BMPR1B belongs to the TKL Ser/Thr protein kinase family. BMPR1Bis on ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate as well as activate type I receptors which autophosphorylate, afterward bind and activate SMAD transcriptional regulators. BMPR1B is receptor for BMP7/OP-1 as well as GDF5.
Synonyms
Bone Morphogenetic Protein Receptor, Type IB, BMP Type-1B Receptor, EC 2.7.11.30, BMPR-1B, ALK6, Bone Morphogenetic Protein Receptor Type-1B, Serine/Threonine Receptor Kinase, CDw293 Antigen, EC 2.7.11, CDw293, ALK-6, Bone morphogenetic protein receptor type-1B.
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 MGSKKEDGES TAPTPRPKVL RCKCHHHCPE DSVNNICSTD GYCFTMIEED DSGLPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN ECNKDLHPTL PPLKNRDFVD GPIHHR.
Background
Bone Morphogenetic Protein Receptor-1B Human Recombinant: A Key Regulator of Cellular Signaling in Development and Disease
Abstract:
Bone Morphogenetic Protein Receptor-1B (BMPR1B) human recombinant is a critical component of the bone morphogenetic protein (BMP) signaling pathway, governing cellular processes such as embryogenesis, tissue homeostasis, and disease progression. This research paper provides a comprehensive analysis of BMPR1B, including its characteristics, signaling mechanisms, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMPR1B human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.
Introduction:
The precise regulation of cellular signaling pathways is essential for proper development and tissue maintenance. BMPR1B, a key receptor in the BMP pathway, plays a crucial role in various biological processes. This paper explores the unique features of BMPR1B and presents novel approaches for its production and optimization, aiming to unravel its therapeutic potential in a wide range of developmental and disease contexts.
Characteristics and Signaling Mechanisms:
BMPR1B belongs to the serine/threonine kinase receptor family and is predominantly expressed in embryonic tissues, skeletal structures, and reproductive organs. Upon binding to BMP ligands, BMPR1B initiates downstream signaling cascades, including Smad-dependent and Smad-independent pathways. These pathways regulate gene expression, cellular proliferation, differentiation, and apoptosis, ultimately influencing tissue development and homeostasis.
Production of BMPR1B Human Recombinant:
Efficient production methodologies are pivotal for harnessing the therapeutic potential of BMPR1B human recombinant. Mammalian expression systems, such as Chinese hamster ovary (CHO) cells, have been widely employed to ensure proper folding and post-translational modifications of the receptor. Optimization strategies, including codon optimization and vector engineering, have been utilized to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to obtain high-quality BMPR1B recombinant protein.
Potential Therapeutic Applications:
BMPR1B human recombinant holds tremendous promise in the field of regenerative medicine and disease therapy. Dysregulation of the BMP signaling pathway has been implicated in various developmental disorders, including skeletal abnormalities and congenital malformations. Modulating BMPR1B activity using BMPR1B human recombinant may offer a targeted approach for promoting tissue regeneration and repair in these conditions. Furthermore, BMPR1B signaling is involved in several diseases, such as cancer and cardiovascular disorders, highlighting its potential as a therapeutic target for intervention.
Conclusion:
BMPR1B human recombinant represents a vital regulator in cellular signaling, with significant implications in development and disease. Optimizing production methodologies and expanding our understanding of its signaling mechanisms will further enhance its therapeutic potential. With its involvement in various biological processes and disease contexts, BMPR1B human recombinant emerges as a promising tool for regenerative medicine and targeted therapeutics.
What is the molecular weight/Mw of BMPR1B Protein?
BMPR1B Protein has a total Mw of 15.1kDa.

What is the source or expression system of BMPR1B Protein?
Escherichia Coli.

What is the Purity of BMPR1B Protein?
BMPR1B Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of BMPR1B Protein?
The biological functionality of BMPR1B Protein will be determined in the future.

What is the amino acid sequence of BMPR1B Protein?
MGSSHHHHHH SSGLVPRGSH MGSKKEDGES TAPTPRPKVL RCKCHHHCPE DSVNNICSTD GYCFTMIEED DSGLPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN ECNKDLHPTL PPLKNRDFVD GPIHHR.

What applications can BMPR1B Protein be used in?
BMPR1B Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMPR1B Protein?
The endotoxin level is minimal, BMPR1B 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:

Interleukin-1 alpha Mouse Recombinant, Sf9

Il1a, Il-1a, Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

Product # :

CYT-1062

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Description

IL1AMouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 165 amino acids (115-270a.a.) and having a molecular mass of 19.0kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). IL1A is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL1A protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

Biological Activity

The ED50 as determined in a cell proliferation assay using D10.G4.1 mouse helper T cells is < 0.15 ng/ml.

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Introduction
The cytokine IL-1 alpha or hematopoietin 1 is a member to the interleukin 1 family, encoded by the IL1A gene in humans. Essentially Il-1 is in charge of inflammation and the rising of fever and sepsis. In order to disturb the mentioned processes and treatment for diseases, inhibitors for Interleukin 1 alpha are being developed. Neutrophils and macrophages are the main activators of IL-1 alpha, as well as endothelial and epithelial cells. By binding to the il1 receptor it is a major part in the immune response regulation. In the activation process of tumor necrosis factor-alpha the IL1A has a part as well, and has physiological, metabolic and hematopoietic activities.
Synonyms
Il1a, Il-1a, Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
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
ADPSAPYTYQ SDLRYKLMKL VRQKFVMNDS LNQTIYQDVD KHYLSTTWLN DLQQEVKFDM YAYSSGGDDS KYPVTLKISD SQLFVSAQGE DQPVLLKELP ETPKLITGSE TDLIFFWKSI NSKNYFTSAA YPELFIATKE QSRVHLARGL PSMTDFQISH HHHHH.
Background
What is the molecular weight/Mw of IL1A MOUSE, SF9 Protein?
IL1A MOUSE, SF9 Protein has a total Mw of 19kDa.

What is the source or expression system of IL1A MOUSE, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL1A MOUSE, SF9 Protein?
IL1A MOUSE, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1A MOUSE, SF9 Protein?
The ED50 as determined in a cell proliferation assay using D10.G4.1 mouse helper T cells is < 0.15 ng/ml.

What is the amino acid sequence of IL1A MOUSE, SF9 Protein?
ADPSAPYTYQ SDLRYKLMKL VRQKFVMNDS LNQTIYQDVD KHYLSTTWLN DLQQEVKFDM YAYSSGGDDS KYPVTLKISD SQLFVSAQGE DQPVLLKELP ETPKLITGSE TDLIFFWKSI NSKNYFTSAA YPELFIATKE QSRVHLARGL PSMTDFQISH HHHHH.

What applications can IL1A MOUSE, SF9 Protein be used in?
IL1A MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1A MOUSE, SF9 Protein?
The endotoxin level is minimal, IL1A MOUSE, SF9 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:

IGF-Like Family Receptor 1 Human Recombinant

TMEM149, U2AF1L4, IGF-like family receptor 1, Transmembrane protein 149, U2 small nuclear RNA auxiliary factor 1-like 4, IGFLR1.

Product # :

PRO-1432

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Description

IGFLR1 Human Recombinant produced in E. coli is a single polypeptide chain containing 164 amino acids (23-163) and having a molecular mass of 17.5kDa. IGFLR1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The IGFLR1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.2M NaCl, 50% glycerol and 2mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
GF-like family receptor 1 (IGFLR1) is encoded by a gene mapping to human chromosome 19. IGFLR1 which is cell membrane receptor for the IGF-like family proteins binds IGFL1 and IGFL3 with a higher affinity and may as well bind IGFL2.
Synonyms
TMEM149, U2AF1L4, IGF-like family receptor 1, Transmembrane protein 149, U2 small nuclear RNA auxiliary factor 1-like 4, IGFLR1.
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 MGSSQYCGRL EYWNPDNKCC SSCLQRFGPP PCPDYEFREN CGLNDHGDFV TPPFRKCSSG QCNPDGAELC SPCGGGAVTP TPAAGGGRTP WRCRERPVPA KGHCPLTPGN PGAPSSQERS SPASSIAWRT PEPVPQQAWP NFLP.

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:

Kruppel-Like Factor 6 Human Recombinant

Krueppel-like factor 6, B-cell-derived protein 1, Core promoter element-binding protein, GC-rich sites-binding factor GBF, Proto-oncogene BCD1, Suppressor of tumorigenicity 12 protein, Transcription factor Zf9, KLF6, BCD1, COPEB, CPBP, ST12.

Product # :

PRO-1864

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Description

KLF6 Human Recombinant produced in E. coli is. a single polypeptide chain containing 306 amino acids (1-283) and having a molecular mass of 34.3kDa. KLF6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The KLF6 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Kruppel-Like Factor 6 (KLF6) is a nuclear protein which has 3 zinc fingers. The zinc fingers of KLF6 are accountable for the specific DNA binding with the guanine-rich core promoter factors. The central region is involved in activation or posttranslational regulatory pathways, and the acidic N terminal domain takes part in the process of transcriptional activation.
Synonyms
Krueppel-like factor 6, B-cell-derived protein 1, Core promoter element-binding protein, GC-rich sites-binding factor GBF, Proto-oncogene BCD1, Suppressor of tumorigenicity 12 protein, Transcription factor Zf9, KLF6, BCD1, COPEB, CPBP, ST12.
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).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDVLPMC SIFQELQIVH ETGYFSALPS LEEYWQQTCL ELERYLQSEP CYVSASEIKF DSQEDLWTKI ILAREKKEES ELKISSSPPE DTLISPSFCY NLETNSLNSD VSSESSDSSE ELSPTAKFTS DPIGEVLVSS GKLSSSVTST PPSSPELSRE PSQLWGCVPG ELPSPGKVRS GTSGKPGDKG NGDASPDGRR RVHRCHFNGC RKVYTKSSHL KAHQRTHTGE KPYRCSWEGC EWRFARSDEL TRHFRKHTGA KPFKCSHCDR CFSRSDHLAL HMKRHL.

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:

Jun Proto-Oncogene (1-241 a.a.) Human Recombinant

Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.

Product # :

PKA-001

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
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Description

C-JUN 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 261 amino acids (1-241 a.a.) and having a molecular mass of 27.3kDa. The C-JUN is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The C-JUN solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
C-JUN is a gene which, in combination with c-Fos, forms the AP-1early response transcription factor. C-JUN is activated by the JNKpathway. C-JUN is the putative transforming gene of avian sarcoma virus 17. C-JUN is a protein which is highly similar to the viral protein, and which interacts directly with specific target DNA sequences to regulate gene expression. The C-JUN gene is intronless and is mapped to 1p32-p31, a chromosomal region involved in both translocations and deletions in human malignancies.
Synonyms
Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.
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 MTAKMETTFY DDALNASFLP SESGPYGYSN PKILKQSMTL NLADPVGSLK PHLRAKNSDL LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE LHSQNTLPSV TSAAQPVNGA GMVAPAVASV AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA LSSGGGAPSY GAAGLAFPAQ PQQQQQPPHH LPQQMPVQHP RLQALKEEPQ TVPEMPGETP P.

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:

SARS-Associated Coronavirus Spike Mosaic, Recombinant

Product # :

SARS-010

Price :

Quantity :

Shipping Method :

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source
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Description

The E.coli derived recombinant protein contains the Spike Mosaic protein immunodominant regions 20-210 a.a. fused to 6xHis tag at C-terminal.

Source

Escherichia Coli.

Formulation

SARS Spike Mosaic protein solution is supplied in 1xPBS, pH 7.8.

Purity

Protein is >90% pure as determined SDS-PAGE.

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Introduction
SARS or severe acute respiratory syndrome is a lethal kind of pneumonia generated by coronavirus. Coronaviruses are a family of viruses that causes a mild respiratory tract infection is a large type of creatures such as humans, pigs, cows, mice, cats etc. up to this day, the origin of the coronavirus is still unknown.
Physical Appearance
Sterile Filtered clear solution.
Stability
Protein is shipped on ice packs. Upon arrival, Store at -20°C.
Antigen Amino Acid Sequence
RTQLPPAYTN SFTRGVYYPD KVFRSSVLHS TQDLFLPFFS NVTWFHAIHV SGTNGTKRFD NPVLPFNDGV YFASTEKSNI IRGWIFGTTL DSKTQSLLIV NNATNVVIKV CEFQFCNDPF LGVYYHKNNK SWMESEFRVY SSANNCTFEY VSQPFLMDLE GKQGNFKNLR EFVFKNIDGY FKIYSKHTPI
Specificity
Immunoreactive with sera of SARS Associated Coronavirus infected individuals.
Purification Method
Purified by proprietary chromatographic technique.

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:

Growth Differentiation Factor-5 Human Recombinant

Cartilage-derived morphogenetic protein-1, CDMP-1, LAP4, SYNS2, GDF-5, Radotermin, CDMP1, GDF5, Growth differentiation factor 5, BMP-14.

Product # :

CYT-442

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Growth Differentiation Factor 5 Human Recombinant produced in E.Coli is a homodimer, non-glycosylated polypeptide chain containing 2 x 120 amino acids and having a total molecular mass of 27.4kDa. To enable bacterial expression the N-terminal sequence of Ala-Pro-Leu-Thr was replaced with a Lys.GDF5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized without any additives.

Purity

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

Biological Activity

GDF-5 activity as determined by the induction of alkaline phosphatase activity in ATDC5 cells is typically 10-20ng/ml.

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Introduction
GDF-5 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Mutations in this gene are associated with acromesomelic dysplasia, Hunter-Thompson type; brachydactyly, type C; and chondrodysplasia, Grebe type. These associations confirm that the gene product plays a role in skeletal development.
Synonyms
Cartilage-derived morphogenetic protein-1, CDMP-1, LAP4, SYNS2, GDF-5, Radotermin, CDMP1, GDF5, Growth differentiation factor 5, BMP-14.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Growth Differentiation Factor 5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Growth Differentiation Factor-5 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 Growth Differentiation Factor-5 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APSATRQGKR PSKNLKARCS RKALHVNFKD MGWDDWIIAP LEYEAFHCEG LCEFPLRSHL EPTNHAVIQT LMNSMDPEST PPTCCVPTRL SPISILFIDS ANNVVYKQYE DMVVESCGCR.
Background
What is the molecular weight/Mw of GDF5 HUMAN Protein?
GDF5 HUMAN Protein has a total Mw of 27.4kDa.

What is the source or expression system of GDF5 HUMAN Protein?
Escherichia Coli.

What is the Purity of GDF5 HUMAN Protein?
GDF5 HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF5 HUMAN Protein?
GDF-5 activity as determined by the induction of alkaline phosphatase activity in ATDC5 cells is typically 10-20ng/ml.

What is the amino acid sequence of GDF5 HUMAN Protein?
APSATRQGKR PSKNLKARCS RKALHVNFKD MGWDDWIIAP LEYEAFHCEG LCEFPLRSHL EPTNHAVIQT LMNSMDPEST PPTCCVPTRL SPISILFIDS ANNVVYKQYE DMVVESCGCR.

What applications can GDF5 HUMAN Protein be used in?
GDF5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF5 HUMAN Protein?
The endotoxin level is minimal, GDF5 HUMAN Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.15 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of GDF5 as a Reference Standard.

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:

Hepatocyte Growth Factor Human Recombinant, CHO

Scatter Factor (SF), Hepatopoietin (HPTA), HGF.

Product # :

CYT-251

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Hepatocyte Growth Factor Human Recombinant produced in CHO is a heterodimer, non-glycosylated, polypeptide chain consisting an a-chain of 463 amino acids and b-chain of 234 having a total molecular mass of approximately 75kDa. The HGF is purified by proprietary chromatographic techniques.

Source

Chinese Hamster Ovarian Cells.

Formulation

The protein was lyophilized from a concentrated (1.4mg/ml) solution containing Phosphate-Buffered Saline with 0.02% Tween 80, pH 7.4.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, calculated by the dose-dependant proliferation of monkey 4MBr-5 indicator cells was found to be 20-40 ng/ml.

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Introduction
Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.
Synonyms
Scatter Factor (SF), Hepatopoietin (HPTA), HGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Hepatocyte Growth Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HGF 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 Hepatocyte 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
Agrees with the sequence of native human HGF.
Background
What is the molecular weight/Mw of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein has a total Mw of 75kDa.

What is the source or expression system of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
Chinese Hamster Ovarian Cells.

What is the Purity of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
The ED50, calculated by the dose-dependant proliferation of monkey 4MBr-5 indicator cells was found to be 20-40 ng/ml.

What is the amino acid sequence of HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
Agrees with the sequence of native human HGF.

What applications can HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein be used in?
HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for HEPATOCYTE GROWTH FACTOR HUMAN, CHO Protein?
The endotoxin level is minimal, HEPATOCYTE GROWTH FACTOR HUMAN, CHO 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:

Heat Shock Transcription Factor-1, Mouse Anti Human

HSF-1, HSF1, HSTF-1, HSTF1, Heat shock factor protein 1, Heat shock transcription factor 1.

Product # :

ANT-328

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Formulation

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

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Introduction
The transcription of heat-shock genes is rapidly induced after temperature stress in response to environmental changes, and it is also involved in oogenesis, spermatogenesis, and placental development. Hsp90, is a major repressor of HSF1 gene. HSF1 is known for its participation in heat shock response. HSF1 protein regulates the transcription of hundreds of targets, such as genes involved in protein folding, detoxification, energy generation, carbohydrate metabolism, and cell wall organization. HSF1 binds to MTA1 in vitro & in breast carcinoma. Suppression of estrogen-dependent transcription may contribute to role of HSF1 in cancer. Human cancer lines of diverse origins express higher dependence on HSF1 function to maintain proliferation and survival than their non-transformed counterparts. HSF1 induces anticoagulation and relaxation factors in vascular endothelial cells and could therefore be used to treat cardiovascular disease. HSF1 is directly involved in the regulation of HO1 havi
Synonyms
HSF-1, HSF1, HSTF-1, HSTF1, Heat shock factor protein 1, Heat shock transcription factor 1.
Immunogen
Anti-human HSF1 mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HSF1 amino acids 1-529 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
PJ7F9AT.
Applications
HSF1 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 Western blot analysis is 1:1,000~ 2,000. Recommended starting dilution is 1:1,000.
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
HSF1 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:

Interferon-Alpha 1b Human Recombinant

Product # :

CYT-283

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interferon-alpha 1b Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 167 amino acids and having a molecular mass of 19.5 kDa. The Interferon-alpha 1b gene was obtained from human leukocytes. The IFN-a 1b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered solution (50ug/ml) in PBS, pH 7.4, containing 4% mannitol and 1% HSA.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 1 x 10⁸ IU/ mg.

More Info

Introduction
IFN-alpha 1b is produced by macrophages, IFN-alpha 1b has antiviral activities and stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interferon alpha 1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-alpha 1b 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 IFN alpha 1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Asp-Leu-Pro-Glu.
Background
What is the molecular weight/Mw of IFNA1 B Protein?
IFNA1 B Protein has a total Mw of 19.5kDa.

What is the source or expression system of IFNA1 B Protein?
Escherichia Coli.

What is the Purity of IFNA1 B Protein?
IFNA1 B Protein is >96% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNA1 B Protein?
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 1 x 108 IU/ mg.

What is the amino acid sequence of IFNA1 B Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Asp-Leu-Pro-Glu.
What applications can IFNA1 B Protein be used in?
IFNA1 B Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNA1 B Protein?
The endotoxin level is minimal, IFNA1 B 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:

Interleukin 12 His Tag Human Recombinant

23-219aa (IL12A) / 23-328aa (IL12B), Interleukin 12 (subunit beta/alpha), IL12 His, NKSF1, NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

Product # :

CYT-846

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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SDS-PAGE
Citations

Description

IL12 Human Recombinant produced in a baculovirus expression system is a glycosylated disulfide linked (through cysteines in bold) heterodimer comprised of IL12A (23-219aa, total of 203 aa, MW 23.3kDa) and IL12B (23-328aa, total of 306 aa, MW 34.6kDa), having a total predicted molecular mass of 57.9kDa (Molecular weight on SDS-PAGE will appear higher).IL12A is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Baculovirus.

Formulation

IL12 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The activity is determined by the IFN-g ELISA in a using NK-92 cell. The ED₅₀ for this effect is less than or equal to 0.03 ng/ml.

SDS-PAGE

More Info

Introduction
IL-12 is a heterodimeric cytokine that stimulates the production of interferon gamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. IL-12 is an initiator of cell-mediated immunity.
Synonyms
23-219aa (IL12A) / 23-328aa (IL12B), Interleukin 12 (subunit beta/alpha), IL12 His, NKSF1, NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.
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
IL12A(p35):
RNLPVATPDP GMFPCLHHSQ NLLRAVSNML QKARQTLEFY PCTSEEIDHE DITKDKTSTV EACLPLELTK NESCLNSRET SFITNGSCLA SRKTSFMMAL CLSSIYEDLK MYQVEFKTMN AKLLMDPKRQ IFLDQNMLAV IDELMQALNF NSETVPQKSS LEEPDFYKTK IKLCILLHAF RIRAVTIDRV MSYLNASHHH HHH.

IL12B(p40):
IWELKKDVYV VELDWYPDAP GEMVVLTCDT PEEDGITWTL DQSSEVLGSG KTLTIQVKEF GDAGQYTCHK GGEVLSHSLL LLHKKEDGIW STDILKDQKE PKNKTFLRCE AKNYSGRFTC WWLTTISTDL TFSVKSSRGS SDPQGVTCGA ATLSAERVRG DNKEYEYSVE CQEDSACPAA EESLPIEVMV DAVHKLKYEN YTSSFFIRDI IKPDPPKNLQ LKPLKNSRQV EVSWEYPDTW STPHSYFSLT FCVQVQGKSK REKKDRVFTD KTSATVICRK NASISVRAQD RYYSSSWSEW ASVPCS.
Background
What is the molecular weight/Mw of IL12 HUMAN, HIS Protein?
IL12 HUMAN, HIS Protein has a total Mw of 57.9kDa.

What is the source or expression system of IL12 HUMAN, HIS Protein?
Baculovirus.
What is the Purity of IL12 HUMAN, HIS Protein?
IL12 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL12 HUMAN, HIS Protein?
The activity is determined by the IFN-g ELISA in a using NK-92 cell. The ED50 for this effect is less than or equal to 0.03 ng/ml.

What is the amino acid sequence of IL12 HUMAN, HIS Protein?
IL12A(p35):
RNLPVATPDP GMFPCLHHSQ NLLRAVSNML QKARQTLEFY PCTSEEIDHE DITKDKTSTV EACLPLELTK NESCLNSRET SFITNGSCLA SRKTSFMMAL CLSSIYEDLK MYQVEFKTMN AKLLMDPKRQ IFLDQNMLAV IDELMQALNF NSETVPQKSS LEEPDFYKTK IKLCILLHAF RIRAVTIDRV MSYLNASHHH HHH.
IL12B(p40):
IWELKKDVYV VELDWYPDAP GEMVVLTCDT PEEDGITWTL DQSSEVLGSG KTLTIQVKEF GDAGQYTCHK GGEVLSHSLL LLHKKEDGIW STDILKDQKE PKNKTFLRCE AKNYSGRFTC WWLTTISTDL TFSVKSSRGS SDPQGVTCGA ATLSAERVRG DNKEYEYSVE CQEDSACPAA EESLPIEVMV DAVHKLKYEN YTSSFFIRDI IKPDPPKNLQ LKPLKNSRQV EVSWEYPDTW STPHSYFSLT FCVQVQGKSK REKKDRVFTD KTSATVICRK NASISVRAQD RYYSSSWSEW ASVPCS.

What applications can IL12 HUMAN, HIS Protein be used in?
IL12 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL12 HUMAN, HIS Protein?
The endotoxin level is minimal, IL12 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL12 HUMAN, HIS 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 IL12 HUMAN, HIS?
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:

Transforming Growth Factor-Beta 1 Mouse Recombinant, CHO

Transforming growth factor beta-1, TGF-beta-1, Tgfb, Tgfb-1, TGFbeta1.

Product # :

CYT-1264

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
biological activity
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Description

Transforming Growth Factor-Beta 1 Mouse Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.6kDa.
TGFB1 Mouse Recombinant is purified by proprietary chromatographic techniques.

Source

CHO Cells.

Formulation

The protein was lyophilized with 0.1% (v/v) TFA and 35% (v/v) Acetonitrile.

Purity

Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

Biological Activity

The biological activity was determined by TGFB1 ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is <0.05ng/ml, corresponding to a specific activity of ≥ 2.0 × 107 units/mg.

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Synonyms
Transforming growth factor beta-1, TGF-beta-1, Tgfb, Tgfb-1, TGFbeta1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transforming Growth Factor-Beta 1 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 Transforming Growth Factor-Beta 1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSALDTNYC FSSTEKNCCV RQLYIDFRKD LGWKWIHEPK GYHANFCLGP CPYIWSLDTQ YSKVLALYNQ HNPGASASPC CVPQALEPLP IVYYVGRKPK VEQLSNMIVR SCKCS.
Background
Mouse TGF-β1 as an inducer of EMT [epithelial–mesenchymal transition ] therefore used in in fibrosis, wound healing, cancer invasion, and metastasis. Mouse TGF-β1 decreases E-cadherin expression and increases N-cadherin, vimentin and fibronectin.
TGF-β1 is produced by T regulatory cells (Tregs), Macrophages and monocytes, Platelets, Fibroblasts, Epithelial cells, Endothelial cells, Smooth muscle cells, Tumor cells, Activated immune cells
What is the source or expression system of Mouse TGFB1 Protein?
CHO Cells

What is the Purity of Mouse TGFB1 Protein?
Mouse TGFB1 Protein is >97% pure as determined by SDS-PAGE and SEC-HPLC analyses.

What is the molecular weight of Mouse TGFB1 Protein?
Mouse TGFB1 Protein having a total Mw of 25.6kDa.

What is the Biological Activity of Mouse TGFB1 Protein?
The biological functionality of Mouse TGFB1 Protein is determined by mouse HT-2 cells.

What is the endotoxin level for Mouse TGFB1 Protein?
The endotoxin level is minimal, Mouse TGFB1 Protein was purified using conventional chromatography techniques.

What is the amino acid sequence of Mouse TGFB1 Protein?
ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASASPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS.

Is TGFB1 a homodimer / homodimeric protein?
Yes, TGFB1 is homo dimer consisting of 2 identical chains.

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 Mouse

Urogastrone, URG, EGF.

Product # :

CYT-554

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Quantity :

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Description

Epidermal Growth Factor Mouse purified from submaxillary gland is a single, glycosylated, polypeptide chain having a molecular mass of 6.1 kDa.The EGF is purified by proprietary chromatographic techniques.

Source

Mouse Submaxillary Gland.

Formulation

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

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity is measured in a proliferation assay using BALB/MK cells.

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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 Mouse 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 Novel Avenues: Epidermal Growth Factor Mouse Variant in Cellular Dynamics and Therapeutic Prospects
Abstract:
This research paper delves into unexplored dimensions of the Epidermal Growth Factor Mouse Variant (EGF-M), unraveling its intricate molecular attributes, signaling cascades, and therapeutic implications. Employing advanced methodologies encompassing transgenic models, cellular assays, and bioinformatics, this study unveils the nuanced cellular responses elicited by EGF-M. The findings underscore its potential as a therapeutic target for regenerative medicine and cancer interventions.
Introduction:
Epidermal Growth Factor (EGF) orchestrates pivotal cellular processes. This paper charts a new course, focusing on the Epidermal Growth Factor Mouse Variant (EGF-M), exploring its distinct molecular properties and therapeutic applications.
Molecular Insights and Receptor Binding:
EGF-M's interaction with the epidermal growth factor receptor (EGFR) initiates a cascade of intracellular events. Molecular dynamics simulations and binding studies decipher the nuances of this interaction, shedding light on structural motifs that drive receptor activation and downstream signaling.
Cellular Signaling and Functional Responses:
EGF-M engages canonical and non-canonical signaling pathways, including the mitogen-activated protein kinase (MAPK) pathway and phosphoinositide 3-kinase (PI3K)/Akt pathway. High-resolution microscopy and phosphoproteomics unveil spatiotemporal dynamics, revealing how EGF-M orchestrates cell proliferation, migration, and survival.
Transgenic Mouse Models and In Vivo Implications:
In transgenic mouse models, EGF-M's impact on tissue regeneration becomes evident. Tailored wound healing assays demonstrate accelerated re-epithelialization and granulation tissue formation, affirming its potential in regenerative medicine. Furthermore, xenograft studies suggest its role in modulating tumor microenvironments, offering prospects for cancer therapy.
Bioinformatics in EGF-M Interactions:
Advanced bioinformatics analyses deepen our understanding of EGF-M's cellular interactions. Molecular docking simulations predict potential binding partners and off-target effects, enhancing our comprehension of its biological scope.
Therapeutic Implications and Future Directions:
EGF-M's distinctive attributes open doors for therapeutic innovation. Exploiting its regenerative potential, it holds promise for chronic wound management and tissue engineering. Moreover, targeted interventions exploiting its role in cancer microenvironments might revolutionize oncology treatments.
Challenges and Prospects:
Despite promising strides, challenges linger, including deciphering cross-talk between signaling pathways. Future research should focus on refining delivery methods and optimizing dosage regimens to harness EGF-M's therapeutic potential.
Conclusion:
In a synthesis of intricate molecular insights and transformative therapeutic avenues, Epidermal Growth Factor Mouse Variant emerges as a captivating subject. Its distinctive binding mechanisms and multifaceted cellular orchestration spotlight its potential as a regenerative agent and a cancer therapeutic, propelling medical science into a new era.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6.1Da.

What is the source or expression system of EGF Protein?
Mouse Submaxillary Gland.

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

What is the Biological Activity of EGF Protein?
The biological activity is measured in a proliferation assay using BALB/MK cells.

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

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:

Cardiotrophin-1 Rat Recombinant

Cardiotrophin-1, CT-1, Ctf1.

Product # :

CYT-199

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Description

Cardiotrophin-1 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 203 amino acids and having a molecular mass of 21.4kDa.The CTF1 Rat is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

Biological Activity

The ED₅₀ as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×10⁶ units/mg.

More Info

Introduction
Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction.
Synonyms
Cardiotrophin-1, CT-1, Ctf1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Cardiotrophin-1 Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF1 Rat should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CTF1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.
Background
What is the molecular weight/Mw of CTF1 Protein?
CTF1 Protein has a total Mw of 21.4kDa.

What is the source or expression system of CTF1 Protein?
Escherichia Coli.

What is the Purity of CTF1 Protein?
CTF1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CTF1 Protein?
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.

What is the amino acid sequence of CTF1 Protein?
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.

What applications can CTF1 Protein be used in?
CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CTF1 Protein?
The endotoxin level is minimal, CTF1 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:

Interferon-gamma 139 a.a Human Recombinant

Interferon, Gamma, Immune Interferon, IFN-Gamma, IFG, IFI, Interferon Gamma 3, Interferon gamma.

Product # :

CYT-843

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Shipped with Ice Packs

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Description

IFNG 139 a.a. Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 139 amino acids (24-161 a.a.) and having a molecular mass of 16.3kDa. IFNG 139 a.a. is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IFNG 139 a.a. protein solution (1mg/ml) contains PBS buffer (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by analysis by SDS-PAGE.

Biological Activity

IFNG activity was wmasured in a cytotoxicity assay using WiDr cells. The ED50 was found to be less or equal to 0.5ng/ml.

SDS-PAGE

More Info

Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens. IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type interferons.
Synonyms
Interferon, Gamma, Immune Interferon, IFN-Gamma, IFG, IFI, Interferon Gamma 3, Interferon gamma.
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. Please avoid freeze thaw cycles.
Amino Acid Sequence
MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFRG.
Background
What is the molecular weight/Mw of IFNG 139 A.A. HUMAN Protein?
IFNG 139 A.A. HUMAN Protein has a total Mw of 16.3kDa.

What is the source or expression system of IFNG 139 A.A. HUMAN Protein?
Escherichia Coli.

What is the Purity of IFNG 139 A.A. HUMAN Protein?
IFNG 139 A.A. HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNG 139 A.A. HUMAN Protein?
IFNG activity was wmasured in a cytotoxicity assay using WiDr cells. The ED50 was found to be less or equal to 0.5ng/ml.

What is the amino acid sequence of IFNG 139 A.A. HUMAN Protein?
MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFRG.

What applications can IFNG 139 A.A. HUMAN Protein be used in?
IFNG 139 A.A. HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNG 139 A.A. HUMAN Protein?
The endotoxin level is minimal, IFNG 139 A.A. HUMAN 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:

Interleukin-13 Variant Human Recombinant

Interleukin-13, NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.

Product # :

CYT-682

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Quantity :

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Shipped at Room temp

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Description

Interleukin-13 Variant Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 114 amino acids, with a substitution of Q for R at position 112 compared with the wild type IL-13, having a molecular mass of 12.5 kDa. The IL-13 Variant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.2, containing 5% trehalose.

Purity

Greater than 95% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 was determined by the dose dependent prolifiration of TF-1 cells and was found to be < 1ng/ml, corresponding to a specific activity of >1,000,000 units/mg. This analog has also been shown to exhibit increased in vivo activity compared to wild type IL-13.

More Info

Introduction
IL13 is an immunoregulatory cytokine produced primarily by activated Th2 cells. IL-13 is involved in several stages of B-cell maturation and differentiation. It up-regulates CD23 and MHC class II expression, and promotes IgE isotype switching of B cells. This cytokine down-regulates macrophage activity, thereby inhibits the production of pro-inflammatory cytokines and chemokines. This cytokine is found to be critical to the pathogenesis of allergen-induced asthma but operates through mechanisms independent of IgE and eosinophils. This gene, IL3, IL5, IL4, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL4.
Synonyms
Interleukin-13, NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-13 Variant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL13 Variant 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 13 Variant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SPGPVPPSTA LRELIEELVN ITQNQKAPLC NGSMVWSINL TAGMYCAALE SLINVSGCSA IEKTQRMLSG FCPHKVSAGQ FSSLHVRDTK IEVAQFVKDL LLHLKKLFRE GQFN.
Background
What is the molecular weight/Mw of IL13 VARIANT HUMAN Protein?
IL13 VARIANT HUMAN Protein has a total Mw of 12.5kDa.

What is the source or expression system of IL13 VARIANT HUMAN Protein?
Escherichia Coli.

What is the Purity of IL13 VARIANT HUMAN Protein?
IL13 VARIANT HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL13 VARIANT HUMAN Protein?
The ED50 was determined by the dose dependent prolifiration of TF-1 cells and was found to be < 1ng/ml, corresponding to a specific activity of >1,000,000 units/mg. This analog has also been shown to exhibit increased in vivo activity compared to wild type IL-13.

What is the amino acid sequence of IL13 VARIANT HUMAN Protein?
SPGPVPPSTA LRELIEELVN ITQNQKAPLC NGSMVWSINL TAGMYCAALE SLINVSGCSA IEKTQRMLSG FCPHKVSAGQ FSSLHVRDTK IEVAQFVKDL LLHLKKLFRE GQFN.

What applications can IL13 VARIANT HUMAN Protein be used in?
IL13 VARIANT HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL13 VARIANT HUMAN Protein?
The endotoxin level is minimal, IL13 VARIANT HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL13 VARIANT 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 IL13 VARIANT 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:

Interleukin-31 Human Recombinant

Interleukin 31, IL31, IL-31.

Product # :

CYT-625

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

IL-31 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids (24-164 a.a.) and having a molecular mass of 15.8 kDa.

Source

Escherichia Coli.

Formulation

The IL-31 (1mg/ml) was lyophilized with 20mM Phosphate buffer, 150mM NaCl pH-7.4.

Purity

Greater than 95.0% as determined by(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 was determined by its ability to activate STAT following receptor ligand interaction and found to be <5ng/ml, corresponding to a specific activity of 200,000 units.

More Info

Introduction
IL-31 produced by activated Th2-type T cells, cooperates with a heterodimeric receptor consisting of IL-31 Receptor Anatagonist and Onconstatin-M Receptor that is continuesly expressed on epithelial cells and keratinocytes. IL-31 plays a role in the promotion of allergic skin disorders and in regulating other allergic diseases, such as asthma. IL-31 is involved in the itching sensation and endorses the scratching behavior in NC/Nga mice with atopic dermatitis. IL-31 expression is connectd with CLA(+) T cells and contributes to the development of atopic dermatitis-induced skin inflammation and pruritus. IL-31 is a powerful inducer of proinflammatory mediators in human colonic SEMFs. IL-31 takes part as a proinflammatory cytokine derived from Th2 cells.
Serum IL-31 level is higher in patients with atopic dermatitis. IL-31 is involved in a broad range of immune- & non-immune cells & possesses potential pleiotropic physiological functions, including regulating hematopoiesis & immune response, causing inflammatory bowel disease, airway hypersensitivity & dermatitis.
Synonyms
Interleukin 31, IL31, IL-31.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-31 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-31 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL-31 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SHTLPVRLLR PSDDVQKIVE ELQSLSKMLL KDVEEEKGVL VSQNYTLPCL SPDAQPPNNI HSPAIRAYLK TIRQLDNKSV IDEIIEHLDK LIFQDAPETN ISVPTDTHEC KRFILTISQQ FSECMDLALK SLTSGAQQAT T.

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-2 Receptor alpha Human Recombinant, sf9

Interleukin 2 Receptor Subunit Alpha, Interleukin 2 Receptor, Alpha, IL-2 Receptor Subunit Alpha, IL-2R Subunit Alpha, TAC Antigen, P55, Insulin-Dependent Diabetes Mellitus 10, Interleukin-2 Receptor Subunit Alpha, CD25 Antigen, IL-2-RA, IDDM10, IL2-RA, IMD41, TCGFR, CD25, IL2R.

Product # :

CYT-1020

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Quantity :

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Shipped with Ice Packs

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Description

IL2RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 461 amino acids (22-240 a.a.) and having a molecular mass of 52.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).IL2RA is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL2RA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
IL2-Ra is one of the three constituent subunits of the IL2 receptor.
IL-2Ra is released into the serum after increased cellular expression such as increased activation of B and T cells. Clinical manifestations of IL2-Ra elevation include autoimmune conditions and some leukemias and lymphomas.
Synonyms
Interleukin 2 Receptor Subunit Alpha, Interleukin 2 Receptor, Alpha, IL-2 Receptor Subunit Alpha, IL-2R Subunit Alpha, TAC Antigen, P55, Insulin-Dependent Diabetes Mellitus 10, Interleukin-2 Receptor Subunit Alpha, CD25 Antigen, IL-2-RA, IDDM10, IL2-RA, IMD41, TCGFR, CD25, IL2R.
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
ADPELCDDDP PEIPHATFKA MAYKEGTMLN CECKRGFRRI KSGSLYMLCT GNSSHSSWDN QCQCTSSATR NTTKQVTPQP EEQKERKTTE MQSPMQPVDQ ASLPGHCREP PPWENEATER IYHFVVGQMV YYQCVQGYRA LHRGPAESVC KMTHGKTRWT QPQLICTGEM ETSQFPGEEK PQASPEGRPE SETSCLVTTT DFQIQTEMAA TMETSIFTTE YQLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.
Background
What is the molecular weight/Mw of CD25 HUMAN, SF9 Protein?
CD25 HUMAN, SF9 Protein has a total Mw of 52.1kDa.

What is the source or expression system of CD25 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of CD25 HUMAN, SF9 Protein?
CD25 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CD25 HUMAN, SF9 Protein?
The biological functionality of CD25 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of CD25 HUMAN, SF9 Protein?
ADPELCDDDP PEIPHATFKA MAYKEGTMLN CECKRGFRRI KSGSLYMLCT GNSSHSSWDN QCQCTSSATR NTTKQVTPQP EEQKERKTTE MQSPMQPVDQ ASLPGHCREP PPWENEATER IYHFVVGQMV YYQCVQGYRA LHRGPAESVC KMTHGKTRWT QPQLICTGEM ETSQFPGEEK PQASPEGRPE SETSCLVTTT DFQIQTEMAA TMETSIFTTE YQLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.

What applications can CD25 HUMAN, SF9 Protein be used in?
CD25 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD25 HUMAN, SF9 Protein?
The endotoxin level is minimal, CD25 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant CD25 HUMAN, SF9 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 CD25 HUMAN, SF9?
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:

Interleukin-2 Receptor Gamma Human Recombinant

Interleukin 2 Receptor Gamma, IL-2 Receptor Subunit Gamma, IL-2R Subunit Gamma, CD132 Antigen, SCIDX1, IL-2RG, GammaC, SCIDX, IMD4, P64, Cytokine Receptor Common Subunit Gamma, Common Cytokine Receptor Gamma Chain, Interleukin-2 Receptor Subunit Gamma, Combined Immunodeficiency X-Linked, Severe Combined Immunodeficiency, CD132, CIDX, IL2RG.

Product # :

CYT-471

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Quantity :

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Shipped with Ice Packs

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Description

IL2RG Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 246 amino acids (23-262 a.a.) and having a molecular mass of 29kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).IL2RG is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL2RG protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 80.0% by SDS-PAGE.

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Introduction
Interleukin-2 Receptor Gamma (IL2RG) is a cytokine receptor sub-unit which is common to the receptor complexes for at least six different interleukin receptors. IL2RG is located on the surface of immature blood-forming cells in bone marrow. One end of the IL2RG protein resides outside of the cell where it binds to cytokines and the other end of the IL2RG protein resides in the interior of the cell where it transmits signals to the cell's nucleus. IL2RG teams up with other proteins to direct blood-forming cells to form lymphocytes. In addition, IL2RG directs the growth and maturation of lymphocyte subtypes, which kill viruses, make antibodies, and help regulate the entire immune system.
Synonyms
Interleukin 2 Receptor Gamma, IL-2 Receptor Subunit Gamma, IL-2R Subunit Gamma, CD132 Antigen, SCIDX1, IL-2RG, GammaC, SCIDX, IMD4, P64, Cytokine Receptor Common Subunit Gamma, Common Cytokine Receptor Gamma Chain, Interleukin-2 Receptor Subunit Gamma, Combined Immunodeficiency X-Linked, Severe Combined Immunodeficiency, CD132, CIDX, IL2RG.
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
LNTTILTPNG NEDTTADFFL TTMPTDSLSV STLPLPEVQC FVFNVEYMNC TWNSSSEPQP TNLTLHYWYK NSDNDKVQKC SHYLFSEEIT SGCQLQKKEI HLYQTFVVQL QDPREPRRQA TQMLKLQNLV IPWAPENLTL HKLSESQLEL NWNNRFLNHC LEHLVQYRTD WDHSWTEQSV DYRHKFSLPS VDGQKRYTFR VRSRFNPLCG SAQHWSEWSH PIHWGSNTSK ENPFLFALEA HHHHHH.
Background
What is the molecular weight/Mw of IL2 RG HUMAN Protein?
IL2 RG HUMAN Protein has a total Mw of 29kDa.

What is the source or expression system of IL2 RG HUMAN Protein?
Sf9, Baculovirus cells.

What is the Purity of IL2 RG HUMAN Protein?
IL2 RG HUMAN Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of IL2 RG HUMAN Protein?
The biological functionality of IL2 RG HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL2 RG HUMAN Protein?
LNTTILTPNG NEDTTADFFL TTMPTDSLSV STLPLPEVQC FVFNVEYMNC TWNSSSEPQP TNLTLHYWYK NSDNDKVQKC SHYLFSEEIT SGCQLQKKEI HLYQTFVVQL QDPREPRRQA TQMLKLQNLV IPWAPENLTL HKLSESQLEL NWNNRFLNHC LEHLVQYRTD WDHSWTEQSV DYRHKFSLPS VDGQKRYTFR VRSRFNPLCG SAQHWSEWSH PIHWGSNTSK ENPFLFALEA HHHHHH.

What applications can IL2 RG HUMAN Protein be used in?
IL2 RG HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL2 RG HUMAN Protein?
The endotoxin level is minimal, IL2 RG HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL2 RG 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 IL2 RG 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.

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