Search: 950 results found for "Natural Coagulation Factors"

Description:

MIG Human Recombinant (CXCL9)

Small inducible cytokine B9, CXCL9, Gamma INF-induced monokine, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, monokine induced by gamma-INF.

Product # :

CHM-333

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Shipped at Room temp

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Description

MIG (monokine induced by gamma-INF) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 103 amino acids and having a molecular mass of 11700 Dalton. The MIG is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 50mM NaCl.

Purity

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

Biological Activity

The biological activity determined by a chemotaxis bioassay using human peripheral blood T-lymphocytes is in a concentration range of 10-100 ng/ml.

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Introduction
Chemokine (C-X-C motif) ligand 9 (CXCL9) is a small cytokine belonging to the CXC chemokine family that is also known as Monokine induced by gamma INF (MIG). CXCL9 is a T-cell chemoattractant, which is induced by IFN-?. It is closely related to two other CXC chemokines called CXCL10 and CXCL11, whose genes are located near the gene for CXCL9 on human chromosome 4. CXCL9, CXCL10 and CXCL11 all elicit their chemotactic functions by interacting with the chemokine receptor CXCR3.
Synonyms
Small inducible cytokine B9, CXCL9, Gamma INF-induced monokine, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, monokine induced by gamma-INF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL9 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 MIG in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TPVVRKGRCSCISTNQGTIHLQSLKDLKQFAPSPSCEKIEIIATLKNGVQTCLNPDS
ADVKELIKKWEKQVSQKKKQKNGKKHQKKKVLKVRKSQRSRQKKTT.
Background
What is the molecular weight/Mw of CXCL9 HUMAN Protein?
CXCL9 HUMAN Protein has a total Mw of 11.7kDa.

What is the source or expression system of CXCL9 HUMAN Protein?
Escherichia Coli.

What is the Purity of CXCL9 HUMAN Protein?
CXCL9 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL9 HUMAN Protein?
The biological activity determined by a chemotaxis bioassay using human peripheral blood T-lymphocytes is in a concentration range of 10-100 ng/ml.

What is the amino acid sequence of CXCL9 HUMAN Protein?
TPVVRKGRCSCISTNQGTIHLQSLKDLKQFAPSPSCEKIEIIATLKNGVQTCLNPDS
ADVKELIKKWEKQVSQKKKQKNGKKHQKKKVLKVRKSQRSRQKKTT.

What applications can CXCL9 HUMAN Protein be used in?
CXCL9 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL9 HUMAN Protein?
The endotoxin level is minimal, CXCL9 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL9 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 CXCL9 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Interleukin-2 Equine Recombinant

Interleukin-2, IL-2, T-cell growth factor, TCGF, IL2.

Product # :

CYT-738

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Description

Recombinant Equine Interleukin-2 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 129 amino acids (with a substitution of S for C - at position 141 compared with the wild type IL2) and having a molecular mass of 14.9kDa.The IL-2 Equine is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 6.0.

Purity

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

Biological Activity

The ED₅₀as determined by a cell proliferation assay using murine CTLL-2 cells is less than 1.0 µg/ml, corresponding to a specific activity of > 1000 IU/mg.

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Introduction
IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.
Synonyms
Interleukin-2, IL-2, T-cell growth factor, TCGF, IL2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL2 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 IL2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APTSSSKRET QQQLKQLQMD LKLLLEGVNN NKNPKLSKML TFKINMPKKA TELKHLQCLE EELKPLEEML KNFLSKDIKE LMSNINVTVL GLKGSETRFT CEYDDETGTI VEFLNKWITF SQSIFSTMT.
Background
What is the molecular weight/Mw of IL 2 EQUINE Protein?
IL 2 EQUINE Protein has a total Mw of 14.9kDa.

What is the source or expression system of IL 2 EQUINE Protein?
Escherichia Coli.

What is the Purity of IL 2 EQUINE Protein?
IL 2 EQUINE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 2 EQUINE Protein?
The ED50 as determined by a cell proliferation assay using murine CTLL-2 cells is less than 1.0 µg/ml, corresponding to a specific activity of > 1000 IU/mg.

What is the amino acid sequence of IL 2 EQUINE Protein?
APTSSSKRET QQQLKQLQMD LKLLLEGVNN NKNPKLSKML TFKINMPKKA TELKHLQCLE EELKPLEEML KNFLSKDIKE LMSNINVTVL GLKGSETRFT CEYDDETGTI VEFLNKWITF SQSIFSTMT.

What applications can IL 2 EQUINE Protein be used in?
IL 2 EQUINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 2 EQUINE Protein?
The endotoxin level is minimal, IL 2 EQUINE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 2 EQUINE 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 IL 2 EQUINE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Interleukin-23 Human Recombinant, His Tag

Interleukin 23 alpha subunit p19, Interleukin-12 subunit beta p40, SGRF, IL23P19, IL-23-A, interleukin-six, G-CSF related factor, JKA3 induced upon T-cell activation, interleukin 12B (natural killer cell stimulatory factor 2 cytotoxic lymphocyte maturation factor 2 p40), NK cell stimulatory factor chain 2, Cytotoxic lymphocyte maturation factor 40 kDa subunit, CLMF2, CLMF p40.

Product # :

CYT-067

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Description

Recombinant Human Interleukin-23 produced in Sf9 Baculovirus cells is a glycosylated heterodimer composed of 2 disulfide-linked subunits. A p19 subunit which is unique to IL23 and a p40 subunit which is shared with IL12. The p19 subunit/IL23A (20-189aa, total of 176 aa, MW 19.5kDa) and p40 subunit /IL12B (23-328aa, total of 306 aa, MW 34.6kDa), the total predicted molecular mass of 54.1kDa (Molecular weight on SDS-PAGE will appear higher). IL23 is fused to a 6 aa His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL23 protein solution (1mg/ml) contains PBS (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by analysis by SDS-PAGE.

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Introduction
IL23 is composed of a subunit of the heterodimeric cytokine IL23 and the p40 subunit of interleukin 12 (IL12B). Interleukin-23 (IL-23) belongs to the IL-12 family and is produced by antigen presenting cells. IL-23 using IL12RB1 and IL-23R (specific for IL-23) can activate STAT and NF-kB pathways and stimulate the production of interferon-gamma. ). IL-23 is known to take a vital part in the inflammation process and is associated with auto immune diseases. However, unlike IL12, which acts primarily on naive CD4(+) T cells, IL23 preferentially acts on memory CD4(+) T cells.
Synonyms
Interleukin 23 alpha subunit p19, Interleukin-12 subunit beta p40, SGRF, IL23P19, IL-23-A, interleukin-six, G-CSF related factor, JKA3 induced upon T-cell activation, interleukin 12B (natural killer cell stimulatory factor 2 cytotoxic lymphocyte maturation factor 2 p40), NK cell stimulatory factor chain 2, Cytotoxic lymphocyte maturation factor 40 kDa subunit, CLMF2, CLMF p40.
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
IL12B: IWELKKDVYV VELDWYPDAP GEMVVLTCDT PEEDGITWTL DQSSEVLGSG KTLTIQVKEF GDAGQYTCHK GGEVLSHSLL LLHKKEDGIW STDILKDQKE PKNKTFLRCE AKNYSGRFTC WWLTTISTDL TFSVKSSRGS SDPQGVTCGA ATLSAERVRG DNKEYEYSVE CQEDSACPAA EESLPIEVMV DAVHKLKYEN YTSSFFIRDI IKPDPPKNLQ LKPLKNSRQV EVSWEYPDTW STPHSYFSLT FCVQVQGKSK REKKDRVFTD KTSATVICRK NASISVRAQD RYYSSSWSEW ASVPCS.
IL23A: RAVPGGSSPA WTQCQQLSQK LCTLAWSAHP LVGHMDLREE GDEETTNDVP HIQCGDGCDP QGLRDNSQFC LQRIHQGLIF YEKLLGSDIF TGEPSLLPDS PVGQLHASLL GLSQLLQPEG HHWETQQIPS LSPSQPWQRL LLRFKILRSL QAFVAVAARV FAHGAATLSP 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:

Inhibin-Alpha A Chain Human Recombinant

Inhibin-Alpha, A-Inhibin Subunit, Inhibin Alpha Chain, INHA.

Product # :

HOR-293

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Description

Inhibin-Alpha A chain Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids fragment (233-366) and having an amino-terminal hexahistidine tag, having a total molecular weight of 19.2 kDa. The Inhibin-Alpha A chain is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

Inhibin-A alpha chain is supplied in 20mM Tris HCl (pH-8), 5mM EDTA and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.
Synonyms
Inhibin-Alpha, A-Inhibin Subunit, Inhibin Alpha Chain, INHA.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
Background
What is the molecular weight/Mw of INHIBIN ALPHA Protein?
INHIBIN ALPHA Protein has a total Mw of 19.2kDa.

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

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

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

What is the amino acid sequence of INHIBIN ALPHA Protein?
INHIBIN ALPHA Protein is composed from 134 amino acids.

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

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

Who supplies recombinant INHIBIN ALPHA 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 INHIBIN ALPHA?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Interleukin-17B Human Recombinant, His Tag

Interleukin-17B, IL-17B, Cytokine Zcyto7, Interleukin-20, Neuronal interleukin-17-related factor, IL20, NIRF, ZCYTO7.

Product # :

CYT-753

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Shipped with Ice Packs

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SDS-PAGE
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Description

IL17B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 185 amino acids (21-180) and having a molecular mass of 20kDa.IL17B is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IL17B solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90.0% by SDS-PAGE.

SDS-PAGE

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Introduction
IL-17 family members are glycoproteins secreted as dimers which induce local cytokine production and recruit granulocytes to sites of inflammation. The IL-17 family is comprised of at least six pro-inflammatory cytokines that share a conserved cysteine-knot structure but diverge at the N-terminus. IL-17 is induced by IL-15 and IL-23, mostly in activated CD4+ T cells distinct from Th1 or Th2 cells. IL-17B binds the IL-17B receptor, but not the IL-17 receptor; it is most homologous with IL-17D, which is expressed by resting CD4+ T cells and CD19+ B cells. IL17B Diseases associated with IL17B include spondyloarthropathy, and neuronitis, and among its related super-pathways are Mucin expression in CF via IL-6, IL-17 signaling pathways and STAT3 Pathway.
Synonyms
Interleukin-17B, IL-17B, Cytokine Zcyto7, Interleukin-20, Neuronal interleukin-17-related factor, IL20, NIRF, ZCYTO7.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMQPRSP KSKRKGQGRP GPLAPGPHQV PLDLVSRMKP YARMEEYERN IEEMVAQLRN SSELAQRKCE VNLQLWMSNK RSLSPWGYSI NHDPSRIPVD LPEARCLCLG CVNPFTMQED RSMVSVPVFS QVPVRRRLCP PPPRTGPCRQ RAVMETIAVG CTCIF.
Background
What is the molecular weight/Mw of IL17B HUMAN, HIS Protein?
IL17B HUMAN, HIS Protein has a total Mw of 20kDa.

What is the source or expression system of IL17B HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of IL17B HUMAN, HIS Protein?
IL17B HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL17B HUMAN, HIS Protein?
The biological functionality of IL17B HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of IL17B HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMQPRSP KSKRKGQGRP GPLAPGPHQV PLDLVSRMKP YARMEEYERN IEEMVAQLRN SSELAQRKCE VNLQLWMSNK RSLSPWGYSI NHDPSRIPVD LPEARCLCLG CVNPFTMQED RSMVSVPVFS QVPVRRRLCP PPPRTGPCRQ RAVMETIAVG CTCIF.

What applications can IL17B HUMAN, HIS Protein be used in?
IL17B HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL17B HUMAN, HIS Protein?
The endotoxin level is minimal, IL17B HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL17B HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL17B HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Inhibin Alpha Human Recombinant

Product # :

HOR-303

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Description

Inhibin-Alpha Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 264 amino acids comprising of both A and B chains, having a molecular mass of 33.5 kDa.The Inhibin-Alpha is fused with an amino-terminal hexahistidine tag. The Inhibin-Alpha is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

Inhibin-A alpha chain is supplied in 20mM Tris and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE analysis.

More Info

Introduction
Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
Amino Acid Sequence
Alpha chain:
STPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIP PNLSLPVPGAPPTPAQPYSLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI.

Beta Chain:
GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMR
GHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.
Background
What is the molecular weight/Mw of INHIBIN A Protein?
INHIBIN A Protein has a total Mw of 33.5kDa.

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

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

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

What is the amino acid sequence of INHIBIN A Protein?
Alpha chain:
STPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIP PNLSLPVPGAPPTPAQPYSLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI.

Beta Chain:
GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMR
GHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.
What applications can INHIBIN A Protein be used in?
INHIBIN A Protein can probably be used in western blot, ELISA and Lateral Flow.

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

Who supplies recombinant INHIBIN A 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 INHIBIN A?
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:

Treponema pallidum p47 (Partial) Recombinant

Product # :

TRP-249

Price :

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Description

The E.Coli derived recombinant protein is fused at the C- terminus with a 6xHis Tag and contains the T.Pallidum p47 immunodominant regions.

Source

Escherichia Coli.

Formulation

70mM Tris-HCl pH8.0, 50mM NaCl, 50% Glycerol and 1.5M urea.

Purity

Treponema Pallidum protein is >95% pure as determined by 10% PAGE (coomassie staining).

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Introduction
Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum subsp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.
Stability
Treponema Pallidum although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Applications
Treponema Pallidum protein is suitable for ELISA and Western blots, excellent antigen for detection of T.Pallidum with minimal specificity problems.
Specificity
Immunoreactive with sera of T.Pallidum infected individuals.
Purification Method
Treponema Pallidum 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:

Hepatitis C Virus NS3 Genotype-6a, (1192-1459 a.a.) Recombinant

Product # :

HCV-211

Price :

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Description

The E.coli derived recombinant protein fused to a His tag contains the HCV NS3 immunodominant regions, amino acids 1192-1459.

Formulation

1.5M urea, 25mM Tris-HCl pH-8, 0.2% Triton-X & 50% Glycerol.

Purity

HCV NS3 Genotype-6a protein is >95% pure as determined by 10% PAGE (coomassie staining).

More Info

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 NS3 Genotype-6a although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Applications
HCV NS3 Genotype-6a antigen is suitable for ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.
Specificity
Immunoreactive with sera of HCV-infected individuals.
Purification Method
HCV NS3 Genotype-6a 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:

YWHAG Mouse Anti Human

14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3 monooxygenase/tryptophan 5-monooxygenase activation protein gamma polypeptide.

Product # :

ANT-539

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Shipped with Ice Packs

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formulation
More Info
Western Blot, ICC/IF
Citations

Formulation

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

Western Blot, ICC/IF

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Introduction
The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms that have been identified in mammals. The 14-3-3gamma, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.
Synonyms
14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3 monooxygenase/tryptophan 5-monooxygenase activation protein gamma polypeptide.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human YWHAG mAb, clone PAT4B9AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human YWHAG protein 1-247 amino acids purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
PAT4B9AT.
Applications
The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
YWHAG antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

Description:

Hepatitis C Virus NS3 Genotype-5, (1192-1459 a.a.) Recombinant

Product # :

HCV-266

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Description

The E.coli derived recombinant protein fused to a His tag contains the HCV NS3 immunodominant regions, amino acids 1192-1459.

Formulation

1.5M urea, 25mM Tris-HCl pH-8, 0.2% Triton-X & 50% Glycerol.

Purity

HCV NS3 Genotype-5 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 NS3 Genotype-5 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Applications
HCV NS3 Genotype-5 antigen in ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.
Specificity
Immunoreactive with sera of HCV-infected individuals.
Purification Method
HCV NS3 Genotype-5 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:

Interferon-gamma 139 a.a Human Recombinant

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

Product # :

CYT-843

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

SDS-PAGE

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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens. IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type interferons.
Synonyms
Interferon, Gamma, Immune Interferon, IFN-Gamma, IFG, IFI, Interferon Gamma 3, Interferon gamma.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
Amino Acid Sequence
MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFRG.
Background
What is the molecular weight/Mw of IFNG 139 A.A. HUMAN Protein?
IFNG 139 A.A. HUMAN Protein has a total Mw of 16.3kDa.

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

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

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

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

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

What is the endotoxin level for IFNG 139 A.A. HUMAN Protein?
The endotoxin level is minimal, IFNG 139 A.A. HUMAN Protein was purified using conventional chromatography techniques.

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

Description:

Midkine Rat Recombinant

Midkine, MK, Mdk.

Product # :

CYT-747

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Shipped at Room temp

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Description

Midkine Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 120 amino acids and having a molecular mass of 13.2kDa.The Midkine Rat 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 determined by a chemotaxis bioassay using human neutrophils is in a concentration range of 10-100 ng/ml.

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Introduction
Midkine (MK) is the product of a retinoic acid responsive gene, MK, and is a member of a family of heparin binding factors. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis.
Synonyms
Midkine, MK, Mdk.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Midkine Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Midkine Rat should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Midkine Rat in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VAKKKDKVKK GSECSEWTWG PCTPSSKDCG MGFREGTCGA QTQRIHCKVP CNWKKEFGAD CKYKFESWGA CDGSTGTKAR QGTLKKARYN AQCQETIRVT KPCTSKTKSK AKAKKGKGKD.

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:

NAD(P)H Dehydrogenase Quinone 1 Human Recombinant

NAD(P)H dehydrogenase (quinone) 1, Quinone reductase 1, QR1, NAD(P)H:quinone oxidoreductase 1, DT-diaphorase, DTD, Azoreductase, Phylloquinone reductase, Menadione reductase, NQO1, DIA4, NMOR1, DHQU, NMORI.

Product # :

ENZ-448

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Description

NQO1 Human Recombinant fused with a 20 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 294 amino acids (1-274 a.a.) and having a molecular mass of 33kDa.The NQO1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NQO1 solution contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
NQO1 belongs to the NAD(P)H dehydrogenase (quinone) family and encodes a cytoplasmic 2-electron reductase. NQO1 acts as an imperative part of cellular antioxidant defense by detoxifying quinines therefore preventing the formation of reactive oxygen species. It seems that NQO1 serves as a quinone reductase relating to conjugation reactions of hydroquinons involved in detoxification pathways in addition to biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. Altered NQO1 expression is seen in many tumors and also linked to Alzheimer’s disease. NQO1 gene mutations are linked to tardive dyskinesia which is an increased risk of hematotoxicity after exposure to benzene, and susceptibility to various forms of cancer.
Synonyms
NAD(P)H dehydrogenase (quinone) 1, Quinone reductase 1, QR1, NAD(P)H:quinone oxidoreductase 1, DT-diaphorase, DTD, Azoreductase, Phylloquinone reductase, Menadione reductase, NQO1, DIA4, NMOR1, DHQU, NMORI.
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 MVGRRALIVL AHSERTSFNY AMKEAAAAAL KKKGWEVVES DLYAMNFNPI ISRKDITGKL KDPANFQYPA ESVLAYKEGH LSPDIVAEQK KLEAADLVIF QFPLQWFGVP AILKGWFERV FIGEFAYTYA AMYDKGPFRS KKAVLSITTG GSGSMYSLQG IHGDMNVILW PIQSGILHFC GFQVLEPQLT YSIGHTPADA RIQILEGWKK RLENIWDETP LYFAPSSLFD LNFQAGFLMK KEVQDEEKNK KFGLSVGHHL GKSIPTDNQI KARK.

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:

Delta Sleep Inducing Peptide

Product # :

HOR-030

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

DSIP Synthetic is a single, non-glycosylated polypeptide chain containing 15 amino acids, having a molecular mass of 1419.55 Dalton and a Molecular formula of C62H98N16O22.

Formulation

The protein was lyophilized with no additives.

Purity

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

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized DSIP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DSIP 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 DSIP 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-Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val-OH
Background
Delta Sleep-Inducing Peptide (DSIP), also known as Sleep-Promoting Peptide, is a neuropeptide that has been the subject of extensive research due to its potential role in sleep regulation, stress response, and neuroprotection. This nonapeptide, first isolated from the cerebral venous blood of rabbits during sleep, has been shown to induce slow-wave sleep, modulate pain perception, and exhibit potential antioxidant and immunomodulatory properties.
DSIP's primary function is its interaction with the sleep regulatory system. By modulating the release of certain neurotransmitters, DSIP can influence sleep patterns, particularly promoting slow-wave sleep, the most restorative stage of sleep. Studies by Kovalzon et al. (2011) have demonstrated that DSIP can enhance sleep quality in rats, suggesting potential applications in sleep disorders and the promotion of healthy sleep patterns.
In addition to its sleep-inducing effects, DSIP has been shown to possess neuroprotective properties. Research by Zolotarev et al. (2014) found that DSIP could protect neurons from oxidative stress, suggesting potential applications in the treatment of neurodegenerative diseases such as Alzheimer's and Parkinson's disease.
Given its sleep-inducing and neuroprotective effects, DSIP has been proposed as a potential therapeutic agent for a variety of conditions, including sleep disorders, chronic pain, and neurodegenerative diseases. For instance, a study by Spong et al. (2016) found that DSIP could improve sleep quality in patients with chronic insomnia, indicating its potential as a therapeutic agent in the treatment of sleep disorders.
While research on DSIP is promising, it is important to note that most studies have been conducted in animals or in vitro. More research is needed to fully understand the potential effects and applications of DSIP in humans. However, the existing body of research suggests that DSIP could be a promising tool in the treatment of sleep disorders, chronic pain, and neurodegenerative diseases.

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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