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Description:

S100 Calcium-Binding Protein A4 Human Recombinant

Protein S100-A4, S100 calcium-binding protein A4, Metastasin, Protein Mts1, Placental calcium-binding protein, Calvasculin, S100A4, CAPL, MTS1, 42A, 18A2, FSP1, P9KA, PEL98.

Product # :

PRO-698

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Description

S100A4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 121 amino acids (1-101) and having a molecular mass of 13.8 kDa.The S100A4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

S100A4 protein at in 20mM Tris-HCl, pH-8 & 10% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
S100A4 is part of the S100 super-family of proteins containing 2 EF-hand calcium binding domains. S100A4 is ubiquitously overexpressed and is localized in the cytoplasm and/or nucleus. S100A4 is involved in motility, invasion, and tubulin polymerization. Chromosomal rearrangements and altered expression of the S100A4 gene have been implicated in tumor metastasis.
Synonyms
Protein S100-A4, S100 calcium-binding protein A4, Metastasin, Protein Mts1, Placental calcium-binding protein, Calvasculin, S100A4, CAPL, MTS1, 42A, 18A2, FSP1, P9KA, PEL98.
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 MACPLEKALD VMVSTFHKYS GKEGDKFKLN KSELKELLTR ELPSFLGKRT DEAAFQKLMS NLDSNRDNEVDFQEYCVFLS CIAMMCNEFF EGFPDKQPRK K.

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:

S100 Calcium Binding Protein A6 Mouse Recombinant

Protein S100-A6, S100 calcium-binding protein A6, Calcyclin, Prolactin receptor-associated protein, 5B10, S100a6, Cacy, 2A9, PRA.

Product # :

PRO-240

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Description

S100A6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (1-89 a.a) and having a molecular mass of 12.2kDa.S100A6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

S100A6 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 100mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
S100A6 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21.
S100A6 may function in stimulation prolactin secretion, and exocytosis. Chromosomal rearrangements and altered expression of the S100A6 gene are implicated in melanoma.
Synonyms
Protein S100-A6, S100 calcium-binding protein A6, Calcyclin, Prolactin receptor-associated protein, 5B10, S100a6, Cacy, 2A9, PRA.
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 MACPLDQAIG LLVAIFHKYS GKEGDKHTLS KKELKELIQK ELTIGSKLQD AEIARLMDDL DRNKDQEVNF QEYVAFLGAL ALIYNEALK.

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:

Macrophage Inflammatory Protein-1 Alpha Mouse Recombinant (CCL3)

Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, L2G25B.

Product # :

CHM-320

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Description

Macrophage Inflammatory Protein-1 alpha Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7820 Dalton. The MIP-1a is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from 1mg/ml solution containing no additives.

Purity

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

Biological Activity

The Activity is calculated by the ability to chemoattract of Balb3/C splenocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

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Introduction
Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.
Synonyms
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, L2G25B.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIP-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL3 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 Macrophage Inflammatory Protein-1a 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, Ala-Pro-Tyr-Gly-Ala.
Background
What is the molecular weight/Mw of MIP 1A MOUSE Protein?
MIP 1A MOUSE Protein has a total Mw of 7.82kDa.

What is the source or expression system of MIP 1A MOUSE Protein?
Escherichia Coli.

What is the Purity of MIP 1A MOUSE Protein?
MIP 1A MOUSE Protein is >99% pure as determined by SDS-PAGE.

What is the Biological Activity of MIP 1A MOUSE Protein?
The Activity is calculated by the ability to chemoattract of Balb3/C splenocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

What is the amino acid sequence of MIP 1A MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Tyr-Gly-Ala.

What applications can MIP 1A MOUSE Protein be used in?
MIP 1A MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for MIP 1A MOUSE Protein?
The endotoxin level is minimal, MIP 1A MOUSE 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:

Actin Rabbit

Product # :

PRO-517

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Description

Ultra pure Actin consists in the alpha-skeletal muscle isoform and is purified from rabbit striated muscle.The purification method used (according to Spudich & Watts) results in a highly purified protein having a Molecular mass of 43,000 dalton.

Source

Rabbit Muscle.

Formulation

The protein was lyophilized from a 1mg/ml solution containing 10mM Tris/HCl buffer pH 8.0, 0.2mM CaCl2, 0.2mM ATP, 1mM DTT and 0.5% (w/v) SDS.

Purity

Greater than 98.0% as determined by SDS-PAGE.

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Introduction
Actin is a muscle protein localized in the I band of the myofibrils; acting along with myosin, it is responsible for contraction and relaxation of muscle. Each actin protomer binds one molecule of ATP and has one high affinity site for either calcium or magnesium ions, as well as several low affinity sites. Actin exists as a monomer in low salt concentrations, but filaments form rapidly as salt concentration rises, with the consequent hydrolysis of ATP. It occurs in globular (G-actin) and fibrous (F-actin) forms. Actin is found in all eukaryotic cells (except for nematode sperm). Actin is one of the most highly-conserved proteins, differing by no more than 20% in species as diverse as algae and humans. Its other functions include cell motility, cell division and cytokinesis, vesicle and organelle movement, cell signaling, and the establishment and maintenance of cell junctions and cell shape.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Store the Lyophilized Actin between 2-8°C, do not freeze. Upon reconstitution Actin 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 Actin in sterile 18MΩ-cm H2O not less than 1mg/ml, which can then be further diluted to other aqueous solutions.

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:

Beta Defensin 118 Human Recombinant

Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.

Product # :

CYT-714

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Description

DEFB118 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (21-123 a.a) and having a molecular mass of 13.8kDa.DEFB118 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

DEFB118 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Beta Defensin 118 (DEFB118) which is a member of the beta subfamily of defensins, is found in a cluster with other beta-defensin genes on the long arm of chromosome 20. Beta-defensins are antimicrobial peptides which provide protection for tissues and organs from infection by a diversity of microorganisms. DEFB118 protein’s expression is regulated by androgen, and the encoded protein binds to sperm and exhibits antibacterial activity.
Synonyms
Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.
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 MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.
Background
Title: Beta Defensin 118 Human Recombinant: Exploring its Role in Innate Immunity and Potential Therapeutic Applications
Abstract:

Beta defensin 118 (BD118) is a member of the beta defensin family, known for its antimicrobial properties and immune-modulatory functions. This research paper provides a comprehensive analysis of human recombinant BD118, focusing on its production, characterization, and potential applications in immune modulation and therapeutic interventions. The paper highlights the significance of BD118 in innate immunity and its role in host defense against microbial pathogens. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD118 in various inflammatory and infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD118 and its utility as a research tool and a potential immunotherapeutic agent.
Introduction:

Beta defensin 118 (BD118) is a small cationic peptide that plays a critical role in the innate immune response against microbial pathogens. Human recombinant BD118, generated through genetic engineering techniques, offers a valuable tool for studying its immune-modulatory properties and exploring its therapeutic potential.
Production and Characterization:

Recombinant BD118 is typically produced using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD118.
Role in Innate Immunity:

BD118 exhibits antimicrobial activity against a wide range of pathogens, including bacteria, fungi, and viruses. Additionally, it possesses immune-modulatory functions, such as the regulation of pro-inflammatory responses and the promotion of wound healing. Recombinant BD118 serves as a valuable tool for investigating the mechanisms underlying its immune-modulatory actions and exploring its potential as an immunotherapeutic agent.
Therapeutic Implications:

Dysregulation of the immune system is associated with various inflammatory and infectious diseases. Recombinant BD118 holds promise as a potential therapeutic agent due to its antimicrobial properties and immune-modulatory functions. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD118 in conditions such as skin infections, respiratory diseases, and inflammatory bowel disease.
Conclusion:

Human recombinant BD118 represents a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in immune modulation contribute to our understanding of innate immunity and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD118 offer promising avenues for improving outcomes in inflammatory and infectious diseases.
What is the molecular weight/Mw of DEFB118 Protein?
DEFB118 Protein has a total Mw of 13.8kDa.

What is the source or expression system of DEFB118 Protein?
Escherichia Coli.

What is the Purity of DEFB118 Protein?
DEFB118 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of DEFB118 Protein?
The biological functionality of DEFB118 Protein will be determined in the future.

What is the amino acid sequence of DEFB118 Protein?
MGSSHHHHHH SSGLVPRGSH MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.

What applications can DEFB118 Protein be used in?
DEFB118 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for DEFB118 Protein?
The endotoxin level is minimal, DEFB118 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:

Annexin A2 Human Recombinant

ANX2, ANX2L4, CAL1H, LIP2, LPC2, LPC2D, P36, PAP-IV, ANXA2, Annexin A2, Annexin-2, Annexin II, Lipocortin II, Calpactin-1 heavy chain, Calpactin I heavy chain, Chromobindin-8, p36, Protein I, Placental anticoagulant protein IV.

Product # :

PRO-777

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Description

ANXA2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 376 amino acids (1-339a.a.) and having a molecular mass of 42.8 kDa. ANXA2 is fused to a 37 amino acid His-Tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ANXA2 (0.5mg/ml) solution containing 20mM Tris-HCl pH-8, 0.1M NaCl and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
ANXA2 is part of the annexin family and is involved in the regulation of cellular growth and in signal transduction pathways. ANXA2 protein functions as an autocrine factor which increases osteoclast formation and bone resorption. ANXA2 is associated with sickle cell osteonecrosis. Reduced ANXA2 expression is associated with osteosarcoma metastases. ANXA2 is part of the putative cell surface vitamin D binding protein binding site complex and functions to mediate the chemotactic cofactor effect. ANXA2 is involved in dysferlin deficiency and in muscular dystrophies. Human colon adenocarcinoma cell differentiation is related with an up-regulation of ANXA2.
Synonyms
ANX2, ANX2L4, CAL1H, LIP2, LPC2, LPC2D, P36, PAP-IV, ANXA2, Annexin A2, Annexin-2, Annexin II, Lipocortin II, Calpactin-1 heavy chain, Calpactin I heavy chain, Chromobindin-8, p36, Protein I, Placental anticoagulant protein IV.
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 KDRWGSHMST VHEILCKLSL EGDHSTPPSA YGSVKAYTNF DAERDALNIE TAIKTKGVDE VTIVNILTNR SNAQRQDIAF AYQRRTKKEL ASALKSALSG HLETVILGLL KTPAQYDASE LKASMKGLGT DEDSLIEIIC SRTNQELQEI NRVYKEMYKT DLEKDIISDT SGDFRKLMVA LAKGRRAEDG SVIDYELIDQ DARDLYDAGV KRKGTDVPKW ISIMTERSVP HLQKVFDRYK SYSPYDMLES IRKEVKGDLE NAFLNLVQCI QNKPLYFADR LYDSMKGKGT RDKVLIRIMV SRSEVDMLKI RSEFKRKYGK SLYYYIQQDT KGDYQKALLY LCGGDD.

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:

Neutrophil Activating Protein-2 Human Recombinant (CXCL7)

Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

Product # :

CHM-274

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Description

Neutrophil Activating Protein-2 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 70 amino acids and having a molecular mass of 7609 Dalton. The NAP-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CXCL7 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

Purity

Greater than 97% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The specific activity as determined by the ability of NAP2 to chemoattract human neurotrophils using a concentration of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

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Introduction
Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.
Synonyms
Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized NAP-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL7should 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 Neutrophil Activating Protein-2in 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 Ala-Glu-Leu-Arg-Cys.
Background
What is the molecular weight/Mw of CXCL7 HUMAN Protein?
CXCL7 HUMAN Protein has a total Mw of 7.6kDa.

What is the source or expression system of CXCL7 HUMAN Protein?
Escherichia Coli.

What is the Purity of CXCL7 HUMAN Protein?
CXCL7 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL7 HUMAN Protein?
The specific activity as determined by the ability of NAP2 to chemoattract human neurotrophils using a concentration of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

What is the amino acid sequence of CXCL7 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Glu-Leu-Arg-Cys.

What applications can CXCL7 HUMAN Protein be used in?
CXCL7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL7 HUMAN Protein?
The endotoxin level is minimal, CXCL7 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:

APRIL Human Recombinant

Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, TNF- and APOL-related leukocyte expressed ligand 2, TALL-2, TNF-related death ligand 1, TRDL-1, CD256, TNFSF13, TALL2, ZTNF2, UNQ383/PRO715.

Product # :

CYT-815

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Description

APRIL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (105-247) and having a molecular mass of 17.6kDa.APRIL is fused to a 16 amino acid T7-tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

APRIL protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
APRIL which is a part of the TNF ligand superfamily (TNFSF13) is a type II transmembrane protein. Normally, APRIL expression is low in tissues, but is elevated in numerous types of tumors and transformed cell lines.
Synonyms
Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, TNF- and APOL-related leukocyte expressed ligand 2, TALL-2, TNF-related death ligand 1, TRDL-1, CD256, TNFSF13, TALL2, ZTNF2, UNQ383/PRO715.
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
MASMTGGQQM GRGSHMAVLT QKQKKQHSVL HLVPINATSK DDSDVTEVMW QPALRRGRGL QAQGYGVRIQ DAGVYLLYSQ VLFQDVTFTM GQVVSREGQG RQETLFRCIR SMPSHPDRAY NSCYSAGVFH LHQGDILSVI IPRARAKLNL SPHGTFLGL.
Background
APRIL Human Recombinant: Expanding the Horizons of Immunotherapy
Abstract:

APRIL (A Proliferation-Inducing Ligand) is a promising molecule within the tumor necrosis factor (TNF) superfamily that plays a pivotal role in immune regulation. This research paper provides an overview of APRIL human recombinant, exploring its potential applications in immunotherapy. Understanding the mechanisms and therapeutic implications of APRIL holds promise in the field of immune-related disorders. This article presents a concise analysis of APRIL, highlighting its potential as a therapeutic target.
Introduction:

Immunotherapy has revolutionized the treatment of various diseases by harnessing the power of the immune system. APRIL, a member of the TNF superfamily, has emerged as a potential candidate for immunotherapeutic interventions. This paper provides an overview of APRIL, shedding light on its structure, function, and potential applications in immunotherapy.
APRIL Structure and Function:

APRIL is a transmembrane protein that can be proteolytically cleaved, leading to the generation of soluble forms. It interacts with its receptors, such as BCMA and TACI, to regulate immune responses. APRIL influences B-cell activation, proliferation, and antibody production, making it a compelling target for immunotherapeutic strategies.
Immunotherapeutic Applications of APRIL Human Recombinant:

APRIL human recombinant holds great potential in immunotherapy. By modulating APRIL activity, it may be possible to enhance immune responses against cancer cells or dampen immune dysregulation in autoimmune disorders. Additionally, APRIL-based therapeutics could be developed to target specific immune cell populations or enhance the efficacy of existing immunotherapies.
Challenges and Future Directions:

Although APRIL shows promise, there are challenges to overcome. Further research is needed to elucidate the precise mechanisms of APRIL-mediated immune regulation and identify optimal therapeutic approaches. Additionally, safety considerations and potential side effects must be thoroughly evaluated.
Conclusion:

APRIL human recombinant represents a valuable tool for advancing immunotherapy. Understanding the structure, function, and therapeutic potential of APRIL opens up new avenues for treating immune-related disorders. Continued research and development in this field have the potential to revolutionize the landscape of immunotherapy, improving patient outcomes and expanding the possibilities for personalized medicine.
What is the molecular weight/Mw of APRIL Protein?
APRIL Protein has a total Mw of 17.6kDa.

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

What is the Purity of APRIL Protein?
APRIL Protein is >85% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of APRIL Protein?
MASMTGGQQM GRGSHMAVLT QKQKKQHSVL HLVPINATSK DDSDVTEVMW QPALRRGRGL QAQGYGVRIQ DAGVYLLYSQ VLFQDVTFTM GQVVSREGQG RQETLFRCIR SMPSHPDRAY NSCYSAGVFH LHQGDILSVI IPRARAKLNL SPHGTFLGL.

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

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

IFN-Beta 1b Human Recombinant

Leukocyte IFN, B cell IFN, Type I IFN, IFNB1, IFB, IFF, IFNB, IFN-b 1b, MGC96956.

Product # :

CYT-234

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Description

IFN beta 1b Human Recombinant produced in E.Coli is a single, non-glycosylated mutein (variant form) of human IFN beta-1b polypeptide chain containing 165 amino acids and having a molecular mass of 18510.86 Dalton.The IFN-beta gene was cloned from human fibroblasts and altered to substitute Serine for the Cysteine residue found at position 17. IFN beta-1b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from 1mg/ml solution containing 50mg Human Albumin & 50mg dextrose.

Purity

Greater than 98.0% 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 (human "Wish" cell line and VSV virus or the monkey VERO cell line with EMCV virus) was found to be 32 x 10⁶ IU/mg.

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Introduction
IFN-beta 1b has antiviral, antibacterial and anticancer activities.
Synonyms
Leukocyte IFN, B cell IFN, Type I IFN, IFNB1, IFB, IFF, IFNB, IFN-b 1b, MGC96956.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFN-beta 1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFNB 1b 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 IFN beta-1b in sterile 18M-cm H2O at a concentration of 0.25mg/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 Ser-Tyr-Asn-Leu-Leu.
Background
What is the molecular weight/Mw of IFN BETA 1B HUMAN Protein?
IFN BETA 1B HUMAN Protein has a total Mw of 18.5kDa.

What is the source or expression system of IFN BETA 1B HUMAN Protein?
Escherichia Coli.

What is the Purity of IFN BETA 1B HUMAN Protein?
IFN BETA 1B HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IFN BETA 1B HUMAN Protein?
The specific activity as determined in a viral resistance assay (human "Wish" cell line and VSV virus or the monkey VERO cell line with EMCV virus) was found to be 32 x 106 IU/mg.

What is the amino acid sequence of IFN BETA 1B HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Tyr-Asn-Leu-Leu.

What applications can IFN BETA 1B HUMAN Protein be used in?
IFN BETA 1B HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFN BETA 1B HUMAN Protein?
The endotoxin level is minimal, IFN BETA 1B 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 1.493 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 calibrated solution of IFN-beta 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:

Interferon-Omega 1 Human Recombinant, HEK

IFN omega-1, IFN alpha-II-1, IFNW1.

Product # :

CYT-1225

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Description

IFNW1 Human Recombinant is a single, glycosylated, polypeptide chain (22-195 a.a) containing a total of 180 amino acids and having a molecular mass of 20.9 kDa. IFNW1 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The IFNW1 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 is ≤0.07 ng/ml, measured in a cytotoxicity assay using TF-1 human erythroleukemic cells .

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Synonyms
IFN omega-1, IFN alpha-II-1, IFNW1.
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
LGCDLPQNHG LLSRNTLVLL HQMRRISPFL CLKDRRDFRF PQEMVKGSQL QKAHVMSVLH EMLQQIFSLF HTERSSAAWN MTLLDQLHTG LHQQLQHLET CLLQVVGEGE SAGAISSPAL TLRRYFQGIR VYLKEKKYSD CAWEVVRMEI MKSLFLSTNM QERLRSKDRD LGSSHHHHHH.
Background
Interferons, a family of signaling proteins, play a pivotal role in the immune system’s defense against viral infections and other threats. Among these, Interferon W1 (IFNW1), a member of the Type I interferon family, has emerged as a key player in orchestrating antiviral responses and modulating immune reactions. This research embarks on a detailed exploration of the IFNW1 protein, unveiling its structural intricacies, signaling pathways, and its broader implications in immune regulation and disease. By delving into IFNW1, scientists aim to comprehend the nuances of its functions, decipher its interactions within the complex interferon network, and explore its potential applications in therapeutic interventions and beyond.
Structural Insights into IFNW1:
IFNW1, like other Type I interferons, exhibits a unique tertiary structure that enables it to interact with specific cell surface receptors. This interaction triggers a cascade of events, leading to the activation of various antiviral genes and immune modulatory pathways. Understanding the structural basis of IFNW1 is crucial for elucidating its binding affinities, biological activities, and its significance in immune responses.
Signaling Pathways and Antiviral Defense:
IFNW1 engages with its cognate receptors, initiating Janus kinase (JAK)-Signal Transducer and Activator of Transcription (STAT) signaling pathways. This activation leads to the transcription of interferon-stimulated genes (ISGs) with potent antiviral properties. IFNW1’s ability to induce an antiviral state in infected and neighboring cells is fundamental for restricting viral replication and curtailing the spread of infections. Additionally, IFNW1 plays a role in modulating adaptive immune responses, contributing to the broader immune defense mechanisms.
IFNW1 in Immunomodulation and Disease:
Beyond its antiviral functions, IFNW1 is implicated in immunomodulation and disease pathogenesis. Dysregulation of IFNW1 signaling is associated with autoimmune disorders, including lupus and rheumatoid arthritis, highlighting its involvement in immune-related diseases. Moreover, IFNW1 is being explored in cancer immunotherapy, where its ability to modulate the tumor microenvironment and enhance immune surveillance presents opportunities for novel treatment strategies.
Therapeutic Potential and Future Prospects:
The unique properties of IFNW1, particularly its role in immune regulation and antiviral defense, position it as a potential therapeutic target. Research efforts are directed towards harnessing its immunomodulatory functions for developing therapies against infectious diseases, autoimmune disorders, and certain cancers. Additionally, understanding IFNW1’s interactions with other components of the immune system opens avenues for innovative approaches in personalized medicine and targeted immunotherapies.
IFNW1 Protein, as an integral component of the interferon network, stands as a sentinel in the body’s defense against viral invasions and immune dysregulations. Its multifaceted roles in antiviral defense, immune modulation, and disease pathogenesis underscore its significance in biology and medicine. As researchers delve deeper into the intricacies of IFNW1, they pave the way for innovative therapies, immunomodulatory interventions, and a deeper understanding of immune responses. This research not only illuminates the pivotal role of IFNW1 but also holds the promise of transformative advancements in medicine, shaping the future of immunology and disease therapeutics.
What is the molecular weight/Mw of IFNW1 HUMAN, HEK Protein?
IFNW1 HUMAN, HEK Protein has a total Mw of 20.9kDa.

What is the source or expression system of IFNW1 HUMAN, HEK Protein?
HEK293 Cells.

What is the Purity of IFNW1 HUMAN, HEK Protein?
IFNW1 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNW1 HUMAN, HEK Protein?
The ED50 is ≤0.07 ng/ml, measured in a cytotoxicity assay using TF-1 human erythroleukemic cells .

What is the amino acid sequence of IFNW1 HUMAN, HEK Protein?
LGCDLPQNHG LLSRNTLVLL HQMRRISPFL CLKDRRDFRF PQEMVKGSQL QKAHVMSVLH EMLQQIFSLF HTERSSAAWN MTLLDQLHTG LHQQLQHLET CLLQVVGEGE SAGAISSPAL TLRRYFQGIR VYLKEKKYSD CAWEVVRMEI MKSLFLSTNM QERLRSKDRD LGSSHHHHHH.

What applications can IFNW1 HUMAN, HEK Protein be used in?
IFNW1 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNW1 HUMAN, HEK Protein?
The endotoxin level is minimal, IFNW1 HUMAN, HEK 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:

Profilin-1 Human Recombinant

Profilin-1, Profilin I, PFN1.

Product # :

PRO-528

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Description

PFN1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 140 amino acids (1-140 a.a.) and having a molecular mass of 15kDa.The PFN1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PFN1 protein solution contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Profilin1 (PFN1) is a ubiquitous actin monomer-binding protein which is a member of the profilin family. PFN1 significantly boosts skin wound healing in-vitro and in-vivo which may be mediated by purinergic receptors. PFN1 is also active in endothelial cell migration and vessel sprouting. PFN1 is thought to control actin polymerization in response to extracellular signals. PFN1 binds to actin and affects the formation of the cytoskeleton. In addition, PFN1 has an important role in the regulation of epithelial cell-cell adhesion. At high concentrations, profilin averts the polymerization of actin, while at low concentrations it enhances the polymerization. PFN1 gene deletion is linked to Miller-Dieker syndrome.
Synonyms
Profilin-1, Profilin I, PFN1.
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
MAGWNAYIDN LMADGTCQDA AIVGYKDSPS VWAAVPGKTF VNITPAEVGV LVGKDRSSFY VNGLTLGGQK CSVIRDSLLQ DGEFSMDLRT KSTGGAPTFN VTVTKTDKTL VLLMGKEGVH GGLINKKCYE MASHLRRSQY.

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:

Prohibitin 2 Human Recombinant

BAP, Bap37, BCAP37, p22, PNAS-141, REA, Prohibitin-2, B-cell receptor-associated protein BAP37, D-prohibitin, Repressor of estrogen receptor activity, PHB2.

Product # :

PRO-1533

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Description

PHB2 Human Recombinant produced in E. coli is a single polypeptide chain containing 322 amino acids (1-299) and having a molecular mass of 35.7kDa. PHB2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PHB2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Prohibitin 2, also known as PHB2, mediates transcriptional repression by nuclear hormone receptors via recruitment of histone deacetylases by similarity. PHB2 functions as an estrogen receptor (ER)-selective coregulator which potentiates the inhibitory activities of antiestrogens and represses the activity of estrogens. PHB2 which is involved in regulating mitochondrial respiration activity and in aging, competes with NCOA1 for modulation of ER transcriptional activity.
Synonyms
BAP, Bap37, BCAP37, p22, PNAS-141, REA, Prohibitin-2, B-cell receptor-associated protein BAP37, D-prohibitin, Repressor of estrogen receptor activity, PHB2.
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 MGSMAQNLKD LAGRLPAGPR GMGTALKLLL GAGAVAYGVR ESVFTVEGGH RAIFFNRIGG VQQDTILAEG LHFRIPWFQY PIIYDIRARP RKISSPTGSK DLQMVNISLR VLSRPNAQEL PSMYQRLGLD YEERVLPSIV NEVLKSVVAK FNASQLITQR AQVSLLIRRE LTERAKDFSL ILDDVAITEL SFSREYTAAV EAKQVAQQEA QRAQFLVEKA KQEQRQKIVQ AEGEAEAAKM LGEALSKNPG YIKLRKIRAA QNISKTIATS QNRIYLTADN LVLNLQDESF TRGSDSLIKG KK.

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:

LD78-beta (CCL3L1) Human Recombinant

C-C motif chemokine 3-like 1, G0/G1 switch regulatory protein 19-2, LD78-beta(1-70), PAT 464.2, Small-inducible cytokine A3-like 1, Tonsillar lymphocyte LD78 beta protein, CCL3L1, D17S1718, G0S19-2, SCYA3L1, LD78, 464.2, SCYA3L, LD78BETA, MGC12815.

Product # :

CHM-263

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Description

CCL3L1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.7kDa. The CCL3L1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

Purity

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

Biological Activity

The biological activity was determined by its ability to chemoattract human monocytes using a concentration range of 1.0-10.0 ng/ml.

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Introduction
CCL3L1 is a small cytokine that belongs to the CC chemokines. The CCL3L1 gene is one of several cytokine genes clustered on the q-arm of chromosome 17. CCL3L1 is involved in immunoregulatory and inflammatory processes. CCL3L1 binds to several chemokine receptors including CCBP2 and CCR5. CCR5 is a co-receptor for HIV, and binding of the CCL3L1 protein to CCR5 inhibits HIV entry.
Synonyms
C-C motif chemokine 3-like 1, G0/G1 switch regulatory protein 19-2, LD78-beta(1-70), PAT 464.2, Small-inducible cytokine A3-like 1, Tonsillar lymphocyte LD78 beta protein, CCL3L1, D17S1718, G0S19-2, SCYA3L1, LD78, 464.2, SCYA3L, LD78BETA, MGC12815.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CCL3L1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL3L1 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 CCL3L1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APLAADTPTA CCFSYTSRQI PQNFIADYFE TSSQCSKPSV IFLTKRGRQV CADPSEEWVQ KYVSDLELSA.
Background
What is the molecular weight/Mw of CCL3L1 HUMAN Protein?
CCL3L1 HUMAN Protein has a total Mw of 7.7kDa.

What is the source or expression system of CCL3L1 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL3L1 HUMAN Protein?
CCL3L1 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL3L1 HUMAN Protein?
The biological activity was determined by its ability to chemoattract human monocytes using a concentration range of 1.0-10.0 ng/ml.

What is the amino acid sequence of CCL3L1 HUMAN Protein?
APLAADTPTA CCFSYTSRQI PQNFIADYFE TSSQCSKPSV IFLTKRGRQV CADPSEEWVQ KYVSDLELSA.

What applications can CCL3L1 HUMAN Protein be used in?
CCL3L1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL3L1 HUMAN Protein?
The endotoxin level is minimal, CCL3L1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL3L1 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 CCL3L1 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:

Furin Human Recombinant

Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.

Product # :

PRO-2199

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Description

FURIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 645 amino acids (108-715 a.a) and having a molecular mass of 69.8kDa. FURIN is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FURIN protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Furin is a member of the peptidase S8 family. Furin signifies the ubiquitous endoprotease activity within constitutive secretory pathwaysas well as capable of cleavage at the RX (K/R) R consensus motif.Furin is considered to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 as well as gp140 and might take part in tumor progression. Among the diseases associated with FURIN are dementia, familial british and plague.
Synonyms
Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMDVY QEPTDPKFPQ QWYLSGVTQR DLNVKAAWAQ GYTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHASCAT CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA GQRLRAGLLP SHLPE.

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:

Cardiac Muscle Troponin T Human Recombinant, His Tag

CMH2, RCM3, TnTC, cTnT, CMPD2, MGC3889, TNNT2, Troponin T- cardiac muscle, Cardiac muscle troponin T, troponin T type 2 (cardiac).

Product # :

PRO-703

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Description

TNNT2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 305 amino acids (1-285 a.a.) and having a molecular mass of 36.4 kDa. The TNNT2 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TNNT2 solution contains 20mM Tris pH-8.0, 50% glycerol, 0.1mM PMSF, 0.5M NaCl, 1mM DTT and 100mM imidazole.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
TNNT2 is the tropomyosin-binding subunit of the troponin complex, which is situated on the thin filament of striated muscles and regulates muscle contraction in response to alterations in intracellular calcium ion concentration. Mutations in TNNT2 gene are related with familial hypertrophic cardiomyopathy as well as with dilated cardiomyopathy. TNNT2 mutation takes part in hypertrophic cardiomyopathy.
Synonyms
CMH2, RCM3, TnTC, cTnT, CMPD2, MGC3889, TNNT2, Troponin T- cardiac muscle, Cardiac muscle troponin T, troponin T type 2 (cardiac).
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).Please prevent freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSDIEEVVEE YEEEEQEEAA VEEQEEAAEE DAEAEAETEE TRAEEDEEEE EAKEAEDGPM EESKPKPRSF MPNLVPPKIP DGERVDFDDI HRKRMEKDLN ELQALIEAHF ENRKKEEEEL VSLKDRIERR RAERAEQQRI RNEREKERQN RLAEERARRE EEENRRKAED EARKKKALSN MMHFGGYIQK TERKSGKRQT EREKKKKILA ERRKVLAIDH LNEDQLREKA KELWQSIYNL EAEKFDLQEK FKQQKYEINV LRNRINDNQK VSKTRGKAKV TGRWK.

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:

Leptin Antagonist Triple Mutant Human Recombinant, Pegylated

Product # :

CYT-702

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Description

Pegylated Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 35.6kDa, Leptin was mutated, resulting in L39A/D40A/F41A. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Leptin Antagonist Triple Mutant Human Recombinant is Mono-Pegylated with 20kDa PEG and was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

Purity

Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.

Biological Activity

Capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake. Its in vivo activity compared to that of PEG-MLA is 9-27 fold higher.

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Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized PEG-SHLA although stable at room temperature for several weeks, should be stored desiccated below - 20C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml of PEG-SHLA and filter sterilization mLEP mutant can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant pegylated Human Recombinant in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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:

Lymphocyte Antigen 6 Complex Locus G6F Human Recombinant

Lymphocyte Antigen 6 Complex Locus G6F, Lymphocyte Antigen 6 Complex Locus G6D, Chromosome 6 Open Reading Frame 21, C6orf21, LY6G6D, NG32, G6F.

Product # :

PRO-1782

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Description

LY6G6F Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 242 amino acids (17-235) and having a molecular mass of 26.2kDa.LY6G6F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The LY6G6F solution contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
The human Lymphocyte Antigen 6 Complex Locus G6F (LY6G6F) protein is a type I transmembrane protein belonging to the immunoglobin (Ig) superfamily, which contains cell-surface proteins involved in the immune system and cellular recognition. The LY6G6F protein has a role in the downstream signal transduction pathways involving GRB2 and GRB7.
Synonyms
Lymphocyte Antigen 6 Complex Locus G6F, Lymphocyte Antigen 6 Complex Locus G6D, Chromosome 6 Open Reading Frame 21, C6orf21, LY6G6D, NG32, G6F.
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 MGSADNMQAI YVALGEAVEL PCPSPPTLHG DEHLSWFCSP AAGSFTTLVA QVQVGRPAPD PGKPGRESRL RLLGNYSLWL EGSKEEDAGR YWCAVLGQHH NYQNWRVYDV LVLKGSQLSA RAADGSPCNV LLCSVVPSRR MDSVTWQEGK GPVRGRVQSF WGSEAALLLV CPGEGLSEPR SRRPRIIRCL MTHNKGVSFS LAASIDASPA LCAPSTGWDM PW

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:

Calponin 1, Basic, Smooth Muscle Human Recombinant

Calponin 1 basic smooth muscle, Calponin H1 smooth muscle, SMCC, Basic calponin, Sm-Calp, calponin-1.

Product # :

PRO-1129

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Shipped with Ice Packs

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Description

CNN1 Human Recombinant produced in E. coli is a single polypeptide chain containing 305 amino acids (1-297) and having a molecular mass of 34.2 kDa.CNN1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The CNN1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
CNN1 is a member of the calponin family. CNN1 is a thin filament-associated protein which is involved in the regulation and modulation of smooth muscle contraction. CNN1 is able to bind to actin, calmodulin, troponin C and tropomyosin. Prevention of actomyosin Mg-ATPase activity is a result of interaction between calponin and actin.
Synonyms
Calponin 1 basic smooth muscle, Calponin H1 smooth muscle, SMCC, Basic calponin, Sm-Calp, calponin-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
MSSAHFNRGP AYGLSAEVKN KLAQKYDHQR EQELREWIEG VTGRRIGNNF MDGLKDGIIL CEFINKLQPG SVKKINESTQ NWHQLENIGN FIKAITKYGV KPHDIFEAND LFENTNHTQV QSTLLALASM AKTKGNKVNV GVKYAEKQER KFEPGKLREG RNIIGLQMGT NKFASQQGMT AYGTRRHLYD PKLGTDQPLD QATISLQMGT NKGASQAGMT APGTKRQIFE PGLGMEHCDT LNVSLQMGSN KGASQRGMTV YGLPRQVYDP KYCLTPEYPE LGEPAHNHHA HNYYNSALEH HHHHH

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:

Vaspin Recombinant Human

Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

Product # :

CYT-1132

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Shipped at Room temp

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Description

Vaspin Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 394 amino acids and having a molecular mass of 45.1kDa. Vaspin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 150mM NaCl and 0.02 % Tween-20.

Purity

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

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Introduction
Vaspin (visceral adipose-specific SERPIN) is a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.
Synonyms
Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Vaspin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Vaspin 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 Vaspin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
LKPSFSPRNY KALSEVQGWK QRMAAKELAR QNMDLGFKLL KKLAFYNPGR NIFLSPLSIS TAFSMLCLGA QDSTLDEIKQ GFNFRKMPEK DLHEGFHYII HELTQKTQDL KLSIGNTLFI DQRLQPQRKF LEDAKNFYSA ETILTNFQNL EMAQKQINDF ISQKTHGKIN NLIENIDPGT VMLLANYIFF RARWKHEFDP NVTKEEDFFL EKNSSVKVPM MFRSGIYQVG YDDKLSCTIL EIPYQKNITA IFILPDEGKL KHLEKGLQVD TFSRWKTLLS RRVVDVSVPR LHMTGTFDLK KTLSYIGVSK IFEEHGDLTK IAPHRSLKVG EAVHKAELKM DERGTEGAAG TGAQTLPMET PLVVKIDKPY LLLIYSEKIP SVLFLGKIVN PIGK.

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:

Pyruvate Kinase I E.Coli Recombinant

Pyruvate kinase I, PK-1, pykF, b1676, JW1666.

Product # :

PKA-028

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Shipping Method :

Shipped with Ice Packs

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Description

pykF E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 494 amino acids (1-470 a.a) and having a molecular mass of 53.3kDa.pykF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

pykF protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
pykF (pyruvate kinase I) is a member of the pyruvate kinase family. pykF is an enzyme involved in glycolysis. pykF catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to ADP, yielding one molecule of pyruvate and one molecule of ATP, a process which also requires a Magnesium ion. This is the final step in the glycolytic pathway, which produces pyruvate molecules, the ultimate product of aerobic glycolysis.
Synonyms
Pyruvate kinase I, PK-1, pykF, b1676, JW1666.
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 MGSHMKKTKI VCTIGPKTES EEMLAKMLDA GMNVMRLNFS HGDYAEHGQR IQNLRNVMSK TGKTAAILLD TKGPEIRTMK LEGGNDVSLK AGQTFTFTTD KSVIGNSEMV AVTYEGFTTD LSVGNTVLVD DGLIGMEVTA IEGNKVICKV LNNGDLGENK GVNLPGVSIA LPALAEKDKQ DLIFGCEQGV DFVAASFIRK RSDVIEIREH LKAHGGENIH IISKIENQEG LNNFDEILEA SDGIMVARGD LGVEIPVEEV IFAQKMMIEK CIRARKVVIT ATQMLDSMIK NPRPTRAEAG DVANAILDGT DAVMLSGESA KGKYPLEAVS IMATICERTD RVMNSRLEFN NDNRKLRITE AVCRGAVETA EKLDAPLIVV ATQGGKSARA VRKYFPDATI LALTTNEKTA HQLVLSKGVV PQLVKEITST DDFYRLGKEL ALQSGLAHKG DVVVMVSGAL VPSGTTNTAS VHVL.

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:

Haptoglobin Human Recombinant

Haptoglobin, HP, BP, HPA1S, MGC111141, HP2-ALPHA-2.

Product # :

PRO-567

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Haptoglobin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing fusion protein with His tag and having a total Mw of 33 kDa (4 kDa His-tag).

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Haptoglobin is a glycoprotein which is synthesized in the liver and circulates in the blood. Haptoglobin is produced typically by hepatocytes but also by other tissues: e.g. skin, lung, and kidney. It is a positive acute phase protein that binds free hemoglobin and removes it from the circulation to prevent kidney injury, and iron loss following hemolysis. The haptoglobin-hemoglobin complex is subsequently removed by the reticuloendothelial system (generally the spleen). As the reticuloendothelial system removes the haptoglobin-hemoglobin complex from the body, haptoglobin levels are reduced in hemolytic anaemias. In the course of binding hemoglobin, haptoglobin sequesters the iron inside hemoglobin, preventing iron-utilizing bacteria from benefitting from hemolysis.
Haptoglobin consists of two A- and two B-chains, connected by disulfide bonds. Three major haptoglobin phenotypes are known to exist (Hp 1-1, Hp 2-1, and Hp 2-2). Hp 1-1 is biologically the most effective in binding free hemoglobin and suppressing inflammatory responses associated with free hemoglobin. Hp 2-2 is biologically the least active, and Hp 2-1 is moderately active. Haptoglobin’s molecular mass ranges from 8-200 kDa.
Reduced levels can be seen in haemolysis and impaired liver function. High levels are a marker for acute or chronic inflammation. Ahaptoglobinemia or hypohaptoglobinemia are caused by mutations in the haptoglobin gene and/or its regulatory regions. Haptoglobin is also linked to diabetic nephropathy, the incidence of coronary artery disease in type 1 diabetes, Crohn's disease, inflammatory disease behavior, primary sclerosing cholangitis, susceptibility to idiopathic Parkinson's disease, and a reduced incidence of Plasmodium falciparum malaria.
Synonyms
Haptoglobin, HP, BP, HPA1S, MGC111141, HP2-ALPHA-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Haptoglobin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Haptoglobin 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 Haptoglobin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
L ILGGHLDAKG SFPWQAKMVS HHNLTTGATL INEQWLLTTA KNLFLNHSEN ATAKDIAPTL TLYVGKKQLV EIEKVVLHPN YSQVDIGLIK LKQKVSVNER VMPICLPSKD YAEVGRVGYV SGWGRNANFK FTDHLKYVML PVADQDQCIR HYEGSTVPEK KTPKSPVGVQ PILNEHTFCA GMSKYQEDTC YGDAGSAFAV HDLEEDTWYA TGILSFDKSC AVAEYGVYVK VTSIQDWVQK TIAEN

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-1b, Mouse Anti-Human Biotin

Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

Product # :

ANT-249

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Quantity :

Shipping Method :

Shipped at Room temp

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Formulation

1 mg/ml in PBS (after reconstitution).

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Introduction
Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.
Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human IL-1b.
Ig Subclass
Mouse IgG2b.
Clone
NYR-hIL1b.
Titer
For intra-cellular staining, 10µl per 1,000,000 cells. By direct ELISA, 1:10,000 dilution will yield >1.0 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Ion Exchange.

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 (CD25), Mouse Anti-Human

CD25, IL2R, TCGFR, IL-2RA, sIL-2RA, TAC antigen, sIL-2R, IDDM10, p55 TypeMouse Anti Human Monoclonal.

Product # :

ANT-104

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Formulation

1mg/ml in PBS (after reconstitution).

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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
CD25, IL2R, TCGFR, IL-2RA, sIL-2RA, TAC antigen, sIL-2R, IDDM10, p55 TypeMouse Anti Human Monoclonal.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
Con A-activated human T cells.
Ig Subclass
Mouse IgG2a.
Clone
YNRhIL2R.
Titer
1:50 dilution will block 70-80% of CTLL proliferative response to 50 units of r.human IL-2 and will stain 70% of PHA-activated human T cells (by FACS) 10µl will stain 106 IL-2R positive cells for FACS analysis or sorting.
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Storage Procedures
In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Ion Exchange.

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:

Helicobacter Pylori Alkyl Hydroperoxide Reductase C Recombinant

Product # :

PRO-369

Price :

Quantity :

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Shipped with Ice Packs

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Description

AhpC recombinant antigen is produced in E. coli expressing the Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) having the Mw of 23 kDa. AhpC recombinant antigen is well recognized by specific IgG and IgM from H. pylori infected patients.

Source

E.Coli

Formulation

The AhpC Pylori recombinant protein is formulated in 1xPBS pH 7.4.

Purity

Greater than 95% pure as determined by 12% PAGE (Coomassie staining).

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Introduction
Helicobacter pylori, a Gram-negative, microaerophilic bacterium that populates in the stomach, predominantly at the antrum. Helicobacter pylori causes a chronic inflammation of the mucoid lining of stomach and is highly related to the growth of duodenal and gastric ulcers and stomach cancer. Over 50% of the world's population harbor H. pylori in their upper gastrointestinal tract, infection is more prevalent in developing countries. Thus far, no ideal target H. pylori antigen has been developed for the diagnostic purpose. 23 kDa H. pylori outer membrane protein was identified with a good sensitivity and coverage in the diagnosis of H. pylori infection.
Physical Appearance
Sterile filtered liquid formulation.
Stability
AhpC although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
MLVTKLAPDFKAPAVLGNNEVDEHFELSKNLGKNGAILFFWP
KDFTFVCPTEIIAFDKRVKDFQEKGFNVIGVSIDSEQVHFAWK
NTPVEKGGIGQVTFPMVADITKSISRDYDVLFEEAIALRGAFLI
DKNMKVRHAVINDLPLGRNADEMLRMVDALLHFEEHGEVCP
AGWRKGDKGMKATHQGVAEYLKENSIKL.
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.

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