Search: 1000 results found for "Inhibin A"

Description:

Interferon-alpha 14 Human Recombinant

Interferon alpha-14, IFN-alpha-14, Interferon alpha-H, LeIF H, Interferon lambda-2-H, IFNA14, LEIF2H, IFN-alphaH.

Product # :

CYT-135

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Description

IFNA14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (24-189 a.a.) and having a molecular mass of 22.4kDa.IFNA14 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IFNA14 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.2M NaCl and 2mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Interferon alpha-14 (IFNA14) is a member of the alpha/beta interferon family. IFNA14 is produced by macrophages (IFN-alpha have antiviral activities). The interferon stimulates the production of 2 enzymes: a protein kinase and an oligoadenylate synthetase.
Synonyms
Interferon alpha-14, IFN-alpha-14, Interferon alpha-H, LeIF H, Interferon lambda-2-H, IFNA14, LEIF2H, IFN-alphaH.
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 MGSHMCNLSQ THSLNNRRTL MLMAQMRRIS PFSCLKDRHD FEFPQEEFDG NQFQKAQAIS VLHEMMQQTF NLFSTKNSSA AWDETLLEKF YIELFQQMND LEACVIQEVG VEETPLMNED SILAVKKYFQ RITLYLMEKK YSPCAWEVVR AEIMRSLSFS TNLQKRLRRK D.
Background
What is the molecular weight/Mw of IFNA14 HUMAN Protein?
IFNA14 HUMAN Protein has a total Mw of 22.4kDa.

What is the source or expression system of IFNA14 HUMAN Protein?
Escherichia Coli.

What is the Purity of IFNA14 HUMAN Protein?
IFNA14 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNA14 HUMAN Protein?
The biological functionality of IFNA14 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IFNA14 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMCNLSQ THSLNNRRTL MLMAQMRRIS PFSCLKDRHD FEFPQEEFDG NQFQKAQAIS VLHEMMQQTF NLFSTKNSSA AWDETLLEKF YIELFQQMND LEACVIQEVG VEETPLMNED SILAVKKYFQ RITLYLMEKK YSPCAWEVVR AEIMRSLSFS TNLQKRLRRK D.

What applications can IFNA14 HUMAN Protein be used in?
IFNA14 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNA14 HUMAN Protein?
The endotoxin level is minimal, IFNA14 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:

Platelet-Derived Growth Factor AA Human Recombinant

Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, PDGF-AA, PDGF-1.

Product # :

CYT-341

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Description

Platelet-Derived Growth Factor AA Human Recombinant is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 125 amino acids and having a total molecular mass of 28511 Dalton. PDGF-AA is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized without any additives.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50, calculated by the dose-dependent proliferation of murine 3T3 indicator cells is < 0.32ng/ml, corresponding to a Specific Activity of 3,125x10³units/mg.

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Introduction
PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGF is stored in platelet alpha-granules and released upon platelet activation. The PDGF is involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGF
have been identified and named PDGFR-alpha and PDGFR-beta. PDGFR-alpha is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-beta interacts with only PDGF-BB and PDGF-AB.
Synonyms
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, PDGF-AA, PDGF-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Platelet-Derived Growth Factor AA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF-AA 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 Platelet-derived Growth Factor-AA in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SIEEAVPAVC KTRTVIYEIP RSQVDPTSAN FLIWPPCVEV KRCTGCCNTS SVKCQPSRVH HRSVKVAKVE YVRKKPKLKE VQVRLEEHLE CACATTSLNP DYREEDTGRP RESGKKRKRK RLKPT.

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:

Insulin Like Growth Factor-1 N15 Labeled Human Recombinant

Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

Product # :

CYT-128

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Description

IGF1 N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 70 amino acids and having a molecular mass of 7.74kDa. The N15 is stable isotope labeled. The IGF1 N15 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IGF1 N15 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

Purity

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

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 10⁵ IU/mg.

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Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGF1 N15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 N15 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 IGF1 N15 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.
Background
What is the molecular weight/Mw of IGF1 N15 HUMAN Protein?
IGF1 N15 HUMAN Protein has a total Mw of 7.74kDa.

What is the source or expression system of IGF1 N15 HUMAN Protein?
Escherichia Coli.

What is the Purity of IGF1 N15 HUMAN Protein?
IGF1 N15 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IGF1 N15 HUMAN Protein?
The ED50 as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg.

What is the amino acid sequence of IGF1 N15 HUMAN Protein?
GPETLCGAEL VDALQFVCGD RGFYFNKPTG YGSSSRRAPQ TGIVDECCFR SCDLRRLEMY CAPLKPAKSA.

What applications can IGF1 N15 HUMAN Protein be used in?
IGF1 N15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IGF1 N15 HUMAN Protein?
The endotoxin level is minimal, IGF1 N15 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:

Macrophage Inflammatory Protein-1 beta Rat Recombinant (CCL4)

C-C motif chemokine 4, Macrophage inflammatory protein 1-beta, MIP-1-beta, Small-inducible cytokine A4, Ccl4, Mip1b, Scya4.

Product # :

CHM-003

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Description

MIP-1b Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 69 amino acids and having a molecular mass of 7.8 kDa. The MIP-1b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 30% Acetonitrile and 0.1% TFA.

Purity

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

Biological Activity

Determined by its ability to chemoattract human monocytes using a concentration range of 0.01-1.0 µg/ml.

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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-1? and MIP-1? 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-? from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.
Synonyms
C-C motif chemokine 4, Macrophage inflammatory protein 1-beta, MIP-1-beta, Small-inducible cytokine A4, Ccl4, Mip1b, Scya4.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Mouse MIP-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse CCL4 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 Mouse MIP-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APIGSDPPTS CCFSYTSRKI HRNFVMDYYE TSSLCSQPAV VFLTKKGRQI CADPSEPWVN EYVNDLELN.
Background
What is the molecular weight/Mw of MIP 1B RAT Protein?
MIP 1B RAT Protein has a total Mw of 7.8kDa.

What is the source or expression system of MIP 1B RAT Protein?
Escherichia Coli.

What is the Purity of MIP 1B RAT Protein?
MIP 1B RAT Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of MIP 1B RAT Protein?
Determined by its ability to chemoattract human monocytes using a concentration range of 0.01-1.0 µg/ml.

What is the amino acid sequence of MIP 1B RAT Protein?
APIGSDPPTS CCFSYTSRKI HRNFVMDYYE TSSLCSQPAV VFLTKKGRQI CADPSEPWVN EYVNDLELN.

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

What is the endotoxin level for MIP 1B RAT Protein?
The endotoxin level is minimal, MIP 1B RAT Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

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:

Collagen Type IV Alpha 3 Binding Protein Human Recombinant

COL4A3BP, FLJ20597, Collagen type IV alpha-3-binding protein, GPBP, STARD11, CERT, HCERT, CERTL, Ceramide Transfer Protein, Goodpasture antigen-binding protein, StAR-related lipid transfer protein 11, START domain-containing protein 11.

Product # :

PRO-837

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Description

COL4A3BP Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 290 amino acids (347-598 a.a.) and having a molecular mass of 33.1 kDa. The COL4A3BP is fused to 38 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

COL4A3BP Human solution containing 20mM Tris HCL pH-8, 0.1M NaCl, & 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
COL4A3BP is a kinase that particularly phosphorylates the N-terminal region of the non-collagenous domain of the alpha 3 chain of type IV collagen, recognized as the Goodpasture antigen that is the outcome of an autoimmune reaction directed at COL4A3BP. One isoform of COL4A3BP participates in ceramide intracellular transport.
Synonyms
COL4A3BP, FLJ20597, Collagen type IV alpha-3-binding protein, GPBP, STARD11, CERT, HCERT, CERTL, Ceramide Transfer Protein, Goodpasture antigen-binding protein, StAR-related lipid transfer protein 11, START domain-containing protein 11.
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 KDRWAGSMLH WPTSLPSGDA FSSVGTHRFV QKVEEMVQNH MTYSLQDVGG DANWQLVVEE GEMKVYRREV EENGIVLDPL KATHAVKGVT GHEVCNYFWN VDVRNDWETT IENFHVVETL ADNAIIIYQT HKRVWPASQR DVLYLSVIRK IPALTENDPE TWIVCNFSVD HDSAPLNNRC VRAKINVAMI CQTLVSPPEG NQEISRDNIL CKITYVANVN PGGWAPASVL RAVAKREYPK FLKRFTSYVQ EKTAGKPILF.

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 A10 (1-162 a.a.) Human Recombinant

anxa-10.

Product # :

PRO-2837

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Quantity :

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Description

The ANXA10 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The ANXA10 His-Tagged Fusion Protein, produced in E. coli, is a 21kDa protein containing 162 amino acid residues of the ANXA10 Human, 1-162 amino acids.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90% as determined by SDS-PAGE.

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Synonyms
anxa-10.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized ANXA10 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Background
Annexin A10 also known as ANXA10 is a part of the annexin family of calcium-binding proteins which members own a conserved core domain and a unique amino-terminal region which may convene binding specificity. The ANXA10 protein contains 4 annexin domains and plays a role in the regulation of cellular growth and signal transduction pathways throughout the cell.

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:

Hepatitis C Virus Core Genotype-1a Recombinant

Product # :

HCV-203

Price :

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Description

The E.coli derived recombinant protein fused to a His tag at C-terminus contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119.

Formulation

1.5M urea, 25mM Tris-HCl pH 8.0, 0.2% tween-20 and 50% Glycerol.

Purity

HCV Core Genotype-1a protein is >95% pure as determined by 10% PAGE (coomassie staining).

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Introduction
HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6).
Stability
HCV Core Genotype-1a although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Specificity
Immunoreactive with sera of HCV-infected individuals.
Purification Method
HCV Core Genotype-1a protein was 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:

Thymopentin

Product # :

HOR-241

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Description

Thymopentin has a molecular formula of C30H49N9O9, Arg-Lys-Asp-Val-Tyr-OH having an Mw of 679.8 Dalton.

Formulation

The protein (1mg/ml) was lyophilized with no additives.

Purity

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

Biological Activity

What is the molecular weight/Mw of THYMOPENTIN Protein? THYMOPENTIN Protein has a total Mw of 0.67kDa. What is the Purity of THYMOPENTIN Protein? THYMOPENTIN Protein is >99% pure as determined by SDS-PAGE. What is the Biological Activity of THYMOPENTIN Protein? The biological functionality of THYMOPENTIN Protein will be determined in the future. What applications can THYMOPENTIN Protein be used in? THYMOPENTIN Protein can probably be used in western blot, ELISA and Lateral Flow. What is the endotoxin level for THYMOPENTIN Protein? The endotoxin level is minimal, THYMOPENTIN Protein was purified using conventional chromatography techniques.

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Introduction
Thymopentin, also known as TP-5, is a synthetic pentapeptide which is the active site of the naturally occurring hormone thymopoietin with immunomodulating properties (corresponding to the amino acids 32-36 of thymopoietin). Thymopentin enhances the production of thymic T cells and may help restore immunocompetence in immunosuppressed subjects. This agent also augments the effects of ionizing radiation by arresting cancer cells in the G2/M phase of the cell cycle.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thymopentin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TP-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 Thymopentin in sterile 18MΩ-cm H2O not less than 100 µg/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:

LL-37

LL37, antibacterial protein LL-37, cathelicidin LL 37, camp.

Product # :

HOR-041

Price :

Quantity :

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Shipped at Room temp

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Description

LL-37 Synthetic is a single, non-glycosylated polypeptide chain containing 37 amino acids, having a molecular mass of 4493 Dalton and a Molecular formula of C205H340N60O53.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

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Synonyms
LL37, antibacterial protein LL-37, cathelicidin LL 37, camp.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized LL-37 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LL-37 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 LL-37 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser-OH.
Background
LL-37, a prominent member of the human cathelicidin family, has emerged as a pivotal host defense peptide with diverse biological functions. This research paper aims to provide a comprehensive analysis of LL-37, elucidating its biochemical properties, antimicrobial activity, immunomodulatory effects, and potential therapeutic applications.
LL-37, derived from the precursor protein hCAP18, plays a crucial role in innate immunity and host defense against microbial pathogens. Beyond its well-established antimicrobial properties, LL-37 exhibits various immunomodulatory effects, making it an intriguing target for therapeutic interventions (Lai & Gallo, 2009). This paper aims to delve into the complexities of LL-37, uncovering its multifaceted nature and potential clinical applications.
LL-37 is a cationic peptide characterized by a helical structure that facilitates its interaction with microbial membranes. Its amphipathic nature enables it to penetrate microbial membranes, leading to disruption and subsequent cell death (Zaiou, 2007). Additionally, LL-37 can undergo proteolytic processing to release smaller bioactive fragments with distinct functions (Bowdish et al., 2005).
LL-37's antimicrobial activity extends beyond direct microbial killing. It also exhibits immunomodulatory effects, stimulating the recruitment of immune cells and promoting the clearance of pathogens through phagocytosis (Scott et al., 2002). Furthermore, LL-37 can neutralize endotoxins, reducing inflammation caused by microbial products (Davidson et al., 2004).
LL-37 possesses immunomodulatory properties that influence various immune cells, including neutrophils, macrophages, dendritic cells, and lymphocytes (Nagaoka et al., 2001). It can promote the differentiation and maturation of immune cells, modulate cytokine production, and contribute to wound healing and tissue repair (van Harten et al., 2018).
The multifunctional nature of LL-37 renders it a promising candidate for various therapeutic applications. LL-37-based therapies are being explored in wound healing, infectious diseases, and immune-related disorders (Pena et al., 2014). Furthermore, LL-37 has shown potential as a vaccine adjuvant, enhancing the immune response to antigens (Howell et al., 2018).
LL-37's diverse roles in immunity and host defense warrant further research to unravel its precise mechanisms of action and potential applications in clinical medicine. As we deepen our understanding of LL-37's complexities, its therapeutic potential continues to expand, offering exciting prospects for the future.

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:

Glucagon Like Peptide-1 (31 a.a.) Human Recombinant

GLP1, GLP2, GRPP.

Product # :

HOR-236

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Description

Glucagon Like Peptide-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 31 amino acids and having a molecular mass of 3.3 kDa. The GLP-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Recombinant GLP-1 concentrated solution (1mg/ml) was lyophilized after extensive dialyses against 0.1mg sodium phosphate monobasic & 1.6mg sodium phosphate dibasic.

Purity

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

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Introduction
Glucagon-like peptide-1 (GLP-1) is derived from the transcription product of the proglucagon gene. The major source of GLP-1 in the body is the intestinal L cell that secretes GLP-1 as a guthormone. The biologically active forms of GLP-1 are: GLP-1-(7-37) and GLP-1-(7-36)NH2.
GLP-1 secretion by L cells is dependent on the presence of nutrients in the lumen of the small intestine. The secretagogues (agents that causes or stimulates secretion) of this hormone include major nutrients like carbohydrate, proteinand lipid. Once in the circulation, GLP-1 has a half life of less than 2 minutes, due to rapid degradation by the enzyme dipeptidyl peptidase-4.
GLP-1 possesses several physiological properties that make it a subject of intensive investigation as a potential treatment of diabetes mellitus. The known physiological functions of GLP-1 include: Increases insulin secretion from the pancreas in a glucose-dependent manner, decreases glucagon secretion from the pancreas, increases beta cells mass and insulin gene expression, inhibits acid secretion and gastric emptying in the stomach, decreases food intake by increasing satiety.
Synonyms
GLP1, GLP2, GRPP.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Glucagon Like Peptide-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GLP-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 Glucagon Like Peptide-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HAEGTFTSDV SSYLEGQAAK EFIAWLVKGR G.
Background
What is the molecular weight/Mw of GLUCAGON-LIKE PEPTIDE1 Protein?
GLUCAGON-LIKE PEPTIDE1 Protein has a total Mw of 3.3kDa.

What is the source or expression system of GLUCAGON-LIKE PEPTIDE1 Protein?
Escherichia Coli.

What is the Purity of GLUCAGON-LIKE PEPTIDE1 Protein?
GLUCAGON-LIKE PEPTIDE1 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of GLUCAGON-LIKE PEPTIDE1 Protein?
The biological functionality of GLUCAGON-LIKE PEPTIDE1 Protein will be determined in the future.

What is the amino acid sequence of GLUCAGON-LIKE PEPTIDE1 Protein?
HAEGTFTSDV SSYLEGQAAK EFIAWLVKGR G.

What applications can GLUCAGON-LIKE PEPTIDE1 Protein be used in?
GLUCAGON-LIKE PEPTIDE1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GLUCAGON-LIKE PEPTIDE1 Protein?
The endotoxin level is minimal, GLUCAGON-LIKE PEPTIDE1 Protein was purified using conventional chromatography techniques.

Who supplies recombinant GLUCAGON-LIKE PEPTIDE1 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 GLUCAGON-LIKE PEPTIDE1?
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:

Allergen Ara h 9.0101 Recombinant

Product # :

ALR-011

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Description

Recombinant Ara h 9.0101 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 9,959 Dalton. Ara h 9.0101 is expressed with a 6xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Sf9 insect cells.

Formulation

Ara h 9.0101 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
LTPs are allergens in plant foods and pollens and are frequently associated with acute reactions in addition to oral allergy syndrome.The lipid transfer protein (LTP) Ara h 9 is a small molecule with high resistance to digestion and heat denaturation.
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. Avoid multiple freeze-thaw cycles.
Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

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:

Tesamorelin

Product # :

HOR-062

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Description

Tesamorelin is a synthetic single, non-glycosylated polypeptide chain containing 44 amino acids, having a molecular mass of 5135.78 Dalton and a Molecular formula of C221H366N72O67S.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tesamorelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Tesamorelin 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 Tesamorelin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
trans-3-hexenoyl-Tyr-Ala-Asp-Ala-IlePhe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-LysLeu-Leu-Gln-Asp-Ile-Met-Ser-Arg-Gln-Gln-Gly-Glu-Ser-Asn-Gln-GluArg-Gly-Ala-Arg-Ala-Arg-Leu-NH2.
Background
Tesamorelin is a growth hormone-releasing hormone (GHRH) analogue. Tesamorelin stimulates the pituitary gland to produce endogenous growth hormone, which targets visceral adipose tissue. Tesamorelin has evolved from a HIV treatment into an effective metabolic and regenerative therapy.

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:

HIV-1 Integrase Recombinant

Product # :

HIV-014

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Description

Recombinant HIV1 Integrase produced in E. coli having a Mw of 30kDa.Recombinant HIV1 Integrase is fused to a 6xHis tag at its C-terminus and purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

HIV1 Integrase solution contains PBS & 25mM K2CO3.

Purity

Protein is >95% pure as determined by 10% PAGE (coomassie staining).

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Physical Appearance
Sterile filtered colorless 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.
Applications
ELISA, WB & LFA.
Background
Human Immunodeficiency Virus type 1 (HIV1) is the causative agent of Acquired Immunodeficiency Syndrome (AIDS), a devastating disease that affects millions of people worldwide. The HIV1 life cycle is a complex process involving several key viral enzymes, one of which is the integrase (IN). HIV1 integrase plays a crucial role in viral replication by catalyzing the integration of viral DNA into the host cell genome, an essential step for the establishment of a persistent infection.
The study of HIV1 integrase has been of great interest to researchers due to its significance as a therapeutic target. In recent years, advances in recombinant DNA technology have allowed for the production and purification of HIV1 integrase in recombinant form, enabling detailed structural and functional studies. This research aims to characterize the HIV1 integrase recombinant and gain insights into its mechanisms of action during viral integration.
The first objective of this study is to express and purify recombinant HIV1 integrase using various expression systems such as bacterial, yeast, or mammalian cell-based systems. Recombinant DNA techniques, including cloning and expression vector design, will be employed to generate the desired constructs for protein production. The recombinant integrase will be purified using affinity chromatography, followed by characterization using biochemical and biophysical techniques.
The second objective is to investigate the enzymatic activity of the purified HIV1 integrase recombinant. In vitro assays will be performed to determine its ability to catalyze the integration of viral DNA into target DNA sequences. Various substrates, including oligonucleotides and plasmids, will be used to assess the substrate specificity and kinetics of the integrase enzyme. Furthermore, the effects of potential inhibitors or small molecules on the enzymatic activity will be evaluated.
The third objective is to elucidate the three-dimensional structure of the HIV1 integrase recombinant using techniques such as X-ray crystallography or cryo-electron microscopy. This structural information will provide valuable insights into the mechanism of integrase function and aid in the rational design of novel inhibitors targeting integrase.
By characterizing the HIV1 integrase recombinant, this research aims to contribute to our understanding of the molecular mechanisms underlying viral integration. The findings from this study may provide crucial information for the development of novel therapeutic strategies targeting HIV1 integrase, potentially leading to the discovery of more effective antiretroviral drugs.

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:

Allergen Fra e 1.0101 Recombinant

Allergen Fra e 1.0101, Fra e 1.0101, Fra e 1.

Product # :

PRO-2286

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Description

Recombinant Allergen Fra e 1.0101 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 17,794 Dalton. Fra e 1.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Sf9 insect cells.

Formulation

Fra e 1.0101 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Allergen Fra e 1.0101 (Fra e 1.0101) causes an allergic reaction in humans.
Synonyms
Allergen Fra e 1.0101, Fra e 1.0101, Fra e 1.
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. Avoid multiple freeze-thaw cycles.
Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
Molar extinction coefficient
14815; A280(1mg/ml)=0.833

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:

Coagulation Factor IX Human

Coagulation factor IX, EC 3.4.21.22, Christmas factor, Plasma thromboplastin component, PTC, F9, FIX, HEMB, MGC129641, MGC129642, GLA domain, Factor IX.

Product # :

PRO-353

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Description

Human Factor-IX produced from fresh frozen human plasma is a glycosylated polypeptide chain having a molecular mass of 56 kDa.

Source

Human Plasma.

Formulation

The Factor-IX is provided in a sterile solution containing 20mM Tris-HCl pH-7.4, 100mM NaCl and 1mM Benzamidine.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The activity per mg was tested and found to be 380 PEU/mg.

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Introduction
Human Factor IX also called Christmas-Factor is a glycoprotein, which is synthesized in the liver and belongs to the serine proteases system and is part of the S1 peptidase family.
Lack of Factor-IX causes Hemophilia-B meaning Christmas Disease. Factor-IX has a N-terminus region which contains 12xGla residues which asist the calcium dpendant binding of Factor-IX to the phospholipid surface. Factor-IX is activated by either factor XIa or the factor VIIa/tissue factor/phospholipid complex. Cleavage yields the intermediate IXa, which is subsequently converted to the fully active form IXab.
Factor-IX binds initially to exosites on the factor XIa heavy chain, followed by interaction at the active site with subsequent bond cleavage. Coagulation factor IX is activated by interaction with the erythrocyte membrane, causing intrinsic coagulation. Chaperones & lectins act simultaniously to guarantee the proper folding of Factor-IX and the retention of mutant molecules. Human Factor IX, activated by either the Contact or Tissue Factor Pathway, is responsible for the activation of Factor X to Xa.
Synonyms
Coagulation factor IX, EC 3.4.21.22, Christmas factor, Plasma thromboplastin component, PTC, F9, FIX, HEMB, MGC129641, MGC129642, GLA domain, Factor IX.
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. Please prevent freeze-thaw cycles..
Human Virus Test
Human plasma was tested and found negative for HIV-1, HIV-2, Hepatitis B Surface antigen and HCV. Donors are screened for CJD (Creutzfeldt-Jakob Disease).

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, Alpha 2, Smooth Muscle, Aorta Human Recombinant

Actin Alpha 2 Smooth Muscle Aorta, Cell Growth-Inhibiting Gene 46 Protein, Actin Aortic Smooth Muscle, Alpha-Cardiac Actin, Alpha-Actin-2, MYMY5, ACTSA, ACTVS, AAT6.

Product # :

PRO-1220

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Description

ACTA2 Human Recombinant produced in E. coli is a single polypeptide chain containing 400 amino acids (3-377) and having a molecular mass of 44.4 kDa.ACTA2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ACTA2 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
ACTA2 is a member of the actin family of proteins, an extremely conserved family of proteins which takes part in cell motility, structure and integrity. Three types of actin isoforms are known: Alpha, beta and gamma. Alpha actins are a main factor of the contractile mechanism, and beta and gamma take part in the regulation of cell motility. ACTA2 is an alpha actin which is located in skeletal muscle. Mutations in ACTA2 cause aortic aneurysm familial thoracic type 6. Various alternatively spliced variants, encoding the same protein were identified.
Synonyms
Actin Alpha 2 Smooth Muscle Aorta, Cell Growth-Inhibiting Gene 46 Protein, Actin Aortic Smooth Muscle, Alpha-Cardiac Actin, Alpha-Actin-2, MYMY5, ACTSA, ACTVS, AAT6.
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 MGSHMEEEDS TALVCDNGSG LCKAGFAGDD APRAVFPSIV GRPRHQGVMV GMGQKDSYVG DEAQSKRGIL TLKYPIEHGI ITNWDDMEKI WHHSFYNELR VAPEEHPTLL TEAPLNPKAN REKMTQIMFE TFNVPAMYVA IQAVLSLYAS GRTTGIVLDS GDGVTHNVPI YEGYALPHAI MRLDLAGRDL TDYLMKILTE RGYSFVTTAE REIVRDIKEK LCYVALDFEN EMATAASSSS LEKSYELPDG QVITIGNERF RCPETLFQPS FIGMESAGIH ETTYNSIMKC DIDIRKDLYA NNVLSGGTTM YPGIADRMQK EITALAPSTM KIKIIAPPER KYSVWIGGSI LASLSTFQQM WISKQEYDEA GPSIVHRKCF.

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:

Ephrin A1 Human Recombinant, Sf9

Ephrin A1, Immediate Early Response Protein B61, TNF Alpha-Induced Protein 4, Ephrin-A1, TNFAIP4, LERK-1, EPLG1, LERK1, Tumor Necrosis Factor, Alpha-Induced Protein 4, Eph-Related Receptor Tyrosine Kinase Ligand 1, EPH-Related Receptor Tyrosine Kinase Ligand 1, Tumor Necrosis Factor Alpha-Induced Protein 4, Ligand Of Eph-Related Kinase 1, ECKLG, EFL1, B61, EPH-related receptor tyrosine kinase ligand 1, LERK-1.

Product # :

PRO-2538

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Description

EFNA1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 406 amino acids (19-182a.a.) and having a molecular mass of 46.6kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).EFNA1 is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

EFNA1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.
Synonyms
Ephrin A1, Immediate Early Response Protein B61, TNF Alpha-Induced Protein 4, Ephrin-A1, TNFAIP4, LERK-1, EPLG1, LERK1, Tumor Necrosis Factor, Alpha-Induced Protein 4, Eph-Related Receptor Tyrosine Kinase Ligand 1, EPH-Related Receptor Tyrosine Kinase Ligand 1, Tumor Necrosis Factor Alpha-Induced Protein 4, Ligand Of Eph-Related Kinase 1, ECKLG, EFL1, B61, EPH-related receptor tyrosine kinase ligand 1, LERK-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
ADPDRHTVFW NSSNPKFRNE DYTIHVQLND YVDIICPHYE DHSVADAAME QYILYLVEHE EYQLCQPQSK DQVRWQCNRP SAKHGPEKLS EKFQRFTPFT LGKEFKEGHS YYYISKPIHQ HEDRCLRLKV TVSGKITHSP QAHVNPQEKR LAADDPEVRV LHSIGHSLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH

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:

CD300A Human Recombinant

CD300a Molecule, CD300a Antigen, IRp60, CD300 Antigen-Like Family Member A, NK Inhibitory Receptor, Immunoglobulin Superfamily Member 12, CMRF35-Like Molecule 8, CMRF35-H, Inhibitory Receptor Protein 60, CMRF-35-H9, CMRF-35H, CLM-8, IRC1, IRC2, CMRF35H Leukocyte Immunoglobulin-Like Receptor, Leukocyte Membrane Antigen, IgSF12.

Product # :

PRO-1618

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Description

CD300A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 134 amino acids (18-128) and having a molecular mass of 14.7kDa.CD300A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CD300A solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
CD300A belongs to the CD300 family and contains 1 Ig-like V-type (immunoglobulin-like) domain. The protein is expressed not only by natural killer (NK) cells but also by T-cell subsets, B-cells, dendritic cells, mast cells, granulocytes and monocytes. CD300A is inhibitory receptor which may contribute to the down-regulation of cytolytic activity in natural killer (NK) cells, and to the down-regulation of mast cell degranulation.
Synonyms
CD300a Molecule, CD300a Antigen, IRp60, CD300 Antigen-Like Family Member A, NK Inhibitory Receptor, Immunoglobulin Superfamily Member 12, CMRF35-Like Molecule 8, CMRF35-H, Inhibitory Receptor Protein 60, CMRF-35-H9, CMRF-35H, CLM-8, IRC1, IRC2, CMRF35H Leukocyte Immunoglobulin-Like Receptor, Leukocyte Membrane Antigen, IgSF12.
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 MGSLSKCRTV AGPVGGSLSV QCPYEKEHRT LNKYWCRPPQ IFLCDKIVET KGSAGKRNGR VSIRDSPANL SFTVTLENLT EEDAGTYWCG VDTPWLRDFH DPVVEVEVSV FPAS

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:

Tissue Plasminogen Activator (311-562 a.a.) Human Recombinant

Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.

Product # :

ENZ-1023

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Description

TPA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 261 amino acids (311-562 a.a.) and having a molecular mass of 29.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).TPA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TPA protein solution (0.5mg/ml) contains 50mM MES (pH 5.0), 5mM CaCl2, 1mM DTT, 0.5M NaCl and 30% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism.
Synonyms
Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.
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
ADPIKGGLFA DIASHPWQAA IFAKHRRSPG ERFLCGGILI SSCWILSAAH CFQERFPPHH LTVILGRTYR VVPGEEEQKF EVEKYIVHKE FDDDTYDNDI ALLQLKSDSS RCAQESSVVR TVCLPPADLQ LPDWTECELS GYGKHEALSP FYSERLKEAH VRLYPSSRCT SQHLLNRTVT DNMLCAGDTR SGGPQANLHD ACQGDSGGPL VCLNDGRMTL VGIISWGLGC GQKDVPGVYT KVTNYLDWIR DNMRPHHHHH H.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Tryptase Alpha/Beta 1 Human Recombinant

Tryptase Alpha/Beta 1, Tryptase Alpha II, Tryptase Beta-1, Tryptase Alpha-1, Tryptase Alpha/Beta-1, Tryptase-I, TPS1, TPS2, TPSB1, Tryptase-III, Mast Cell Alpha II Tryptase, Mast Cell Beta I Tryptase, EC 3.4.21.59.

Product # :

ENZ-652

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Shipped with Ice Packs

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Description

TPSAB1 Human Recombinant produced in E. coli is a single polypeptide chain containing 270 amino acids (31-275) and having a molecular mass of 30.1 kDa.TPSAB1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TPSAB1 solution (1mg/1ml) 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
Tryptase alpha/beta-1 (TPSAB1) is a tryptase which is the key neutral protease present in mast cells and is discharged upon the coupled activation-degranulation response of this cell type. TPSAB1 is enzymatically active only as a heparin-stabilized tetramer, and is resistant to all known endogenous proteinase inhibitors. TPSAB1 is implicated as a mediator in the pathogenesis of asthma and other allergic and inflammatory disorders.
Synonyms
Tryptase Alpha/Beta 1, Tryptase Alpha II, Tryptase Beta-1, Tryptase Alpha-1, Tryptase Alpha/Beta-1, Tryptase-I, TPS1, TPS2, TPSB1, Tryptase-III, Mast Cell Alpha II Tryptase, Mast Cell Beta I Tryptase, EC 3.4.21.59.
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 MGSHMIVGGQ EAPRSKWPWQ VSLRVHGPYW MHFCGGSLIH PQWVLTAAHC VGPDVKDLAA LRVQLREQHL YYQDQLLPVS RIIVHPQFYT AQIGADIALL ELEEPVNVSS HVHTVTLPPA SETFPPGMPC WVTGWGDVDN DERLPPPFPL KQVKVPIMEN HICDAKYHLG AYTGDDVRIV RDDMLCAGNT RRDSCQGDSG GPLVCKVNGT WLQAGVVSWG EGCAQPNRPG IYTRVTYYLD WIHHYVPKKP.

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:

Protein Phosphatase 1, Regulatory Subunit 8 Human Recombinant

Protein phosphatase 1 regulatory subunit 8, nuclear inhibitor of protein phosphatase-1 alpha, Protein phosphatase 1 regulatory inhibitor subunit 8, ARD1, NIPP1, PRO2047, ARD-1, activator of RNA decay, nuclear subunit of PP-1, RNase E.

Product # :

ENZ-648

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Description

PPP1R8 Human Recombinant produced in E. coli is a single polypeptide chain containing 359 amino acids (1-351) and having a molecular mass of 39.5 kDa.PPP1R8 is fused to a 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The PPP1R8 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Protein Phosphatase 1, Regulatory Subunit 8 (PPP1R8) is the RNA-binding subunit of a key species of protein phosphatase-1 in the nucleus. The PPP1R8 enzyme is an inhibitor subunit of the main nuclear protein phosphatase-1 (PP-1). PPP1R8 has RNA-binding activity however it doesn’t cleave RNA and may target PP-1 to RNA-associated substrates. Two isoforms of the PPP1R8 protein are specific inhibitors of type 1 serine/threonine protein phosphatases which can bind but not cleave RNA. The third isoform of the PPP1R8 protein is deficient in of the phosphatase inhibitory activity nonetheless it is a single-strand endoribonuclease comparable to RNase E of E. coli.
Synonyms
Protein phosphatase 1 regulatory subunit 8, nuclear inhibitor of protein phosphatase-1 alpha, Protein phosphatase 1 regulatory inhibitor subunit 8, ARD1, NIPP1, PRO2047, ARD-1, activator of RNA decay, nuclear subunit of PP-1, RNase E.
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
MAAAANSGSS LPLFDCPTWA GKPPPGLHLD VVKGDKLIEK LIIDEKKYYL FGRNPDLCDF TIDHQSCSRV HAALVYHKHL KRVFLIDLNS THGTFLGHIR LEPHKPQQIP IDSTVSFGAS TRAYTLREKP QTLPSAVKGD EKMGGEDDEL KGLLGLPEEE TELDNLTEFN TAHNKRISTL TIEEGNLDIQ RPKRKRKNSR VTFSEDDEII NPEDVDPSVG RFRNMVQTAV VPVKKKRVEG PGSLGLEESG SRRMQNFAFS GGLYGGLPPT HSEAGSQPHG IHGTALIGGL PMPYPNLAPD VDLTPVVPSA VNMNPAPNPA VYNPEAVNEP KKKKYAKEAW PGKKPTPSLL IVEHHHHHH

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:

Ribose 5-Phosphate Isomerase A Human Recombinant

Ribose-5-phosphate isomerase, Phosphoriboisomerase, RPIA, RPI.

Product # :

ENZ-228

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Shipped with Ice Packs

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Description

RPIA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-311) and having a molecular mass of 35.4kDa.RPIA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RPIA solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT,40% glycerol, 200mM NaCl, 2mM EDTA and 0.2mM PMSF.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Ribose-5-phosphate isomerase (RPIA) is a member of the ribose 5-phosphate isomerase family. RPIA is an enzyme which catalyzes the conversion between ribose-5-phosphate (R5P) and ribulose-5-phosphate (Ru5P). RPI occurs as 2 separate proteins forms, termed RPIA and RPIB. RPIA has a vital role in the metabolism of plants and animals, as it is involved in the Calvin cycle which takes place in plants, and the pentose phosphate pathway which occurs in plants as well as animals.
Synonyms
Ribose-5-phosphate isomerase, Phosphoriboisomerase, RPIA, RPI.
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 MQRPGPFSTL YGRVLAPLPG RAGGAASGGG GNSWDLPGSH VRLPGRAQSG TRGGAGNTST SCGDSNSICP APSTMSKAEE AKKLAGRAAV ENHVRNNQVL GIGSGSTIVH AVQRIAERVK QENLNLVCIP TSFQARQLIL QYGLTLSDLD RHPEIDLAID GADEVDADLN LIKGGGGCLT QEKIVAGYAS RFIVIADFRK DSKNLGDQWH KGIPIEVIPM AYVPVSRAVS QKFGGVVELR MAVNKAGPVV TDNGNFILDW KFDRVHKWSE VNTAIKMIPG VVDTGLFINM AERVYFGMQD GSVNMREKPF C.

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 Rat Recombinant

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-381

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Shipping Method :

Shipped at Room temp

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Description

Interleukin-1A Rat Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 155 amino acids and having a molecular mass of 17703 Dalton. The IL-1A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 50mM Tris-HCl, pH=8.

Purity

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

Biological Activity

The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.005 ng/ml, corresponding to a Specific Activity of 200,000,000IU/mg.

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Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
Synonyms
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 White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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 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-His-Ser-Phe.
Background
What is the molecular weight/Mw of IL1A RAT Protein?
IL1A RAT Protein has a total Mw of 17.7kDa.

What is the source or expression system of IL1A RAT Protein?
Escherichia Coli.

What is the Purity of IL1A RAT Protein?
IL1A RAT Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1A RAT Protein?
The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.005 ng/ml, corresponding to a Specific Activity of 200,000,000IU/mg.

What is the amino acid sequence of IL1A RAT Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-His-Ser-Phe.

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

What is the endotoxin level for IL1A RAT Protein?
The endotoxin level is minimal, IL1A RAT Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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