Search: 1000 results found for "interleukin"

Description:

Angiopoietin-like Protein 3 (243-460 a.a.) Human Recombinant

Angiopoietin-Like 3, ANGPT5, Angiopoietin 5, FHBL2, ANG-5, Angiopoietin-Related Protein 3, Angiopoietin-Like Protein 3, Angiopoietin-5, ANL3, Angiopoietin-related protein 3.

Product # :

CYT-902

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Description

ANGPTL3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 239 amino acids (243-460 a.a) and having a molecular mass of 27.7kDa. ANGPTL3 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

ANGPTL3 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

sds-page

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Introduction
ANGPTL3 and ANGPTL4 are angiopoietin-like proteins secreted and expressed mainly by the liver, their role being the regulation of triglyceride metabolism by inhibiting the lipolysis of triglyceride-rich lipoproteins. During different nutritional states (feeding/fasting) the levels of the circulating triglycerides are regulated by Angptl3 and Angptl4 through differential inhibition of Lipoprotein lipase (LPL) as shown by the experimental data. The molecular structure of ANGPTL3 is similar to that of the angiopoietins (vascular endothelial growth factors). Deletion mutants of human Angiopoietin 5 were used in order to demonstrate that the N-terminal domain (fragment 17-207) and not the C-terminal fibrinogen-like domain (fragment 207-460) increased the plasma triglyceride levels in mice.
Synonyms
Angiopoietin-Like 3, ANGPT5, Angiopoietin 5, FHBL2, ANG-5, Angiopoietin-Related Protein 3, Angiopoietin-Like Protein 3, Angiopoietin-5, ANL3, Angiopoietin-related protein 3.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPAECTTIYN RGEHTSGMYA IRPSNSQVFH VYCDVISGSP WTLIQHRIDG SQNFNETWEN YKYGFGRLDG EFWLGLEKIY SIVKQSNYVL RIELEDWKDN KHYIEYSFYL GNHETNYTLH LVAITGNVPN AIPENKDLVF STWDHKAKGH FNCPEGYSGG WWWHDECGEN NLNGKYNKPR AKSKPERRRG LSWKSQNGRL YSIKSTKMLI HPTDSESFE.
Background
What is the molecular weight/Mw of ANGPTL3 Protein?
ANGPTL3 Protein has a total Mw of 27.7kDa.

What is the source or expression system of ANGPTL3 Protein?
Escherichia Coli.

What is the Purity of ANGPTL3 Protein?
ANGPTL3 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of ANGPTL3 Protein?
The biological functionality of ANGPTL3 Protein will be determined in the future.

What is the amino acid sequence of ANGPTL3 Protein?
MGSSHHHHHH SSGLVPRGSH MPAECTTIYN RGEHTSGMYA IRPSNSQVFH VYCDVISGSP WTLIQHRIDG SQNFNETWEN YKYGFGRLDG EFWLGLEKIY SIVKQSNYVL RIELEDWKDN KHYIEYSFYL GNHETNYTLH LVAITGNVPN AIPENKDLVF STWDHKAKGH FNCPEGYSGG WWWHDECGEN NLNGKYNKPR AKSKPERRRG LSWKSQNGRL YSIKSTKMLI HPTDSESFE.

What applications can ANGPTL3 Protein be used in?
ANGPTL3 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for ANGPTL3 Protein?
The endotoxin level is minimal, ANGPTL3 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:

Insulin Like Growth Factor Binding Protein-3 Human Recombinant, His Tag

Insulin-like growth factor-binding protein 3, Insulin Like Growth Factor Binding Protein-3, His Tag, IGFBP3, IBP-3, IGF-binding protein 3, IGFBP-3, IBP3, BP-53, Insulin-like growth factor binding protein 3 isoform b precursor.

Product # :

CYT-879

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Description

IGFBP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 285 amino acids (28-291a.a.) and having a molecular mass of 31kDa.IGFBP3 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IGFBP3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

Purity

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

SDS-PAGE

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Introduction
IGFBP3 is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein forms a ternary complex with insulin-like growth factor acid-labile subunit (IGFALS) and either insulin-like growth factor (IGF) I or II. In this form, it circulates in the plasma, prolonging the half-life of IGFs and altering their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
Synonyms
Insulin-like growth factor-binding protein 3, Insulin Like Growth Factor Binding Protein-3, His Tag, IGFBP3, IBP-3, IGF-binding protein 3, IGFBP-3, IBP3, BP-53, Insulin-like growth factor binding protein 3 isoform b precursor.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGASSAGLGP VVRCEPCDAR ALAQCAPPPA VCAELVREPG CGCCLTCALS EGQPCGIYTE RCGSGLRCQP SPDEARPLQA LLDGRGLCVN ASAVSRLRAY LLPAPPAPGN ASESEEDRSA GSVESPSVSS THRVSDPKFH PLHSKIIIIK KGHAKDSQRY KVDYESQSTD TQNFSSESKR ETEYGPCRRE MEDTLNHLKF LNVLSPRGVH IPNCDKKGFY KKKQCRPSKG RKRGFCWCVD KYGQPLPGYT TKGKEDVHCY SMQSK.
Background
What is the molecular weight/Mw of IGFBP3 HUMAN, HIS Protein?
IGFBP3 HUMAN, HIS Protein has a total Mw of 31kDa.

What is the source or expression system of IGFBP3 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of IGFBP3 HUMAN, HIS Protein?
IGFBP3 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IGFBP3 HUMAN, HIS Protein?
The biological functionality of IGFBP3 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of IGFBP3 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGASSAGLGP VVRCEPCDAR ALAQCAPPPA VCAELVREPG CGCCLTCALS EGQPCGIYTE RCGSGLRCQP SPDEARPLQA LLDGRGLCVN ASAVSRLRAY LLPAPPAPGN ASESEEDRSA GSVESPSVSS THRVSDPKFH PLHSKIIIIK KGHAKDSQRY KVDYESQSTD TQNFSSESKR ETEYGPCRRE MEDTLNHLKF LNVLSPRGVH IPNCDKKGFY KKKQCRPSKG RKRGFCWCVD KYGQPLPGYT TKGKEDVHCY SMQSK.

What applications can IGFBP3 HUMAN, HIS Protein be used in?
IGFBP3 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IGFBP3 HUMAN, HIS Protein?
The endotoxin level is minimal, IGFBP3 HUMAN, HIS 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:

Beta Defensin-3 Mouse Recombinant

Beta-defensin 3, BD-3, mBD-3, Defensin beta 3, Defb3, Bd3, MGC129397.

Product # :

CYT-036

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Description

Beta Defensin-3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of 4.6kDa. The BD-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Mouse BD-3 was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.

Purity

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

Biological Activity

Measured by its antimicrobial activity against E. coli. The ED₅₀ for this effect is typically 4-20µg/ml, corresponding to a specific activity of 50,000-250,000units/mg.

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Introduction
Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.
Synonyms
Beta-defensin 3, BD-3, mBD-3, Defensin beta 3, Defb3, Bd3, MGC129397.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Beta Defensin-3 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-3 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 Beta Defensin-3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
KKINNPVSCL RKGGRCWNRC IGNTRQIGSC GVPFLKCCKR K.
Background
What is the molecular weight/Mw of BD3 Protein?
BD3 Protein has a total Mw of 4.6kDa.

What is the source or expression system of BD3 Protein?
Escherichia Coli.

What is the Purity of BD3 Protein?
BD3 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of BD3 Protein?
Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 4-20µg/ml, corresponding to a specific activity of 50,000-250,000units/mg.

What is the amino acid sequence of BD3 Protein?
KKINNPVSCL RKGGRCWNRC IGNTRQIGSC GVPFLKCCKR K.

What applications can BD3 Protein be used in?
BD3 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD3 Protein?
The endotoxin level is minimal, BD3 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:

Globular Adiponectin Human Recombinant

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-615

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Description

gAcrp30 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 145 amino acids and having a molecular mass of 16.7kDa. The gAcrp30 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Sterile filtered and lyophilized from 10mM sodium phosphate & 0.5mM DTT, pH 7.5.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

gAcrp30 activity is determined by its ability to inhibit the proliferation of mouse M1 cells. The expected ED₅₀ for this effect is 669ng/ml, corresponding to a specific activity of 1.5x10³units/mg.

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Introduction
gAcrp30 globular protein, exists as a result of proteolytic processing of adiponectin. Adiponectin is manufactured and secreted solely by adipocytes, and is a highly obtained plasma protein, accounting for up to 0.05% of total serum protein. Similar to Adiponectin, gAcrp30 is able of lowering hyperglycemia and reversing INS resistance. In addition, gAcrp30 is an significant protein that is involved in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids. AdipoR1 & AdipoR2 are the 2 signaling receptors for adiponectin and gAcrp30 that were recently been identified.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Stability
For long term, store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time two weeks.
Solubility
We recommended reconstituting gAcrp30 at a concentration of 0.1mg per ml with 10mM sodium phosphate & 0.5mM DTT, pH 7.5. which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MKGEPGEGAY VYRSAFSVGL ETYVTIPNMP IRFTKIFYNQ QNHYDGSTGK FHCNIPGLYY FAYHITVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTN.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16.7kDa.

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

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

What is the Biological Activity of ADIPONECTIN Protein?
gAcrp30 activity is determined by its ability to inhibit the proliferation of mouse M1 cells. The expected ED50 for this effect is 669ng/ml, corresponding to a specific activity of 1.5x103units/mg.

What is the amino acid sequence of ADIPONECTIN Protein?
MKGEPGEGAY VYRSAFSVGL ETYVTIPNMP IRFTKIFYNQ QNHYDGSTGK FHCNIPGLYY FAYHITVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTN.

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

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

Tumor Necrosis Factor-alpha, Mouse-Anti Human

TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

Product # :

ANT-124

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesisand viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human TNF-a.
Ig Subclass
Mouse IgG1.
Clone
NYRhTNFa-E2.
Applications
Direct ELISA, Western Blot, Immuneprecipitation, Intracellular staining.
Note
This antibody will bind very well to protein A in a buffer (PBS) containing high salt concentration (3M Nacl).
Titer
In direct ELISA, using alkaline phosphatase goat anti-mouse Ig (Jackson Laboratories) 1:10,000 dilution will yield 0.7 O.D within 10 minutes.
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
Purification Method
ion exchange.

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

Description:

Leukocyte Immunoglobulin Like Receptor B2 Human Recombinant

Leukocyte Immunoglobulin-like Receptor, CD85D, CD85d, CD85 antigen-like family member D, CD85d antigen, ILT-4, ILT4, ILT4CD85d, Ig-like transcript 4, Immunoglobulin-like transcript 4, LILRB2, LIR2, LIR-2, LIR2CD85D, Leukocyte immunoglobulin-like receptor 2, MIR10, MIR-10, MIR10LILRA6, Monocyte/macrophage immunoglobulinlike receptor 10, leukocyte immunoglobulin-like receptor subfamily B member 2, leukocyte immunoglobulin-like receptor subfamily B member 2 soluble isoform 1.

Product # :

PRO-2729

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Description

LILRB2 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 444 amino acids (24-461 a.a) and having a molecular mass of 48.3kDa.LILRB2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The LILRB2 solution (0. 5mg/ml) contains phosphate buffered saline (pH7.4) and 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Leukocyte Immunoglobulin Like Receptor B2 (LILRB2) is a member of the leukocyte immunoglobulin-like receptor (LIR) family. LILRB2is expressed on immune cells where it binds to MHC class I molecules on antigen-presenting cells and transduces a negative signal that inhibits stimulation of an immune response.LILRB2controls inflammatory responses and cytotoxicity to help focus the immune response and limit autoreactivity.LILRB2competes with CD8 alpha for MHC I binding. LILRB2binds to classical MHC I proteins as well as the non-classical HLA-G1 and HLA-F molecules.
Synonyms
Leukocyte Immunoglobulin-like Receptor, CD85D, CD85d, CD85 antigen-like family member D, CD85d antigen, ILT-4, ILT4, ILT4CD85d, Ig-like transcript 4, Immunoglobulin-like transcript 4, LILRB2, LIR2, LIR-2, LIR2CD85D, Leukocyte immunoglobulin-like receptor 2, MIR10, MIR-10, MIR10LILRA6, Monocyte/macrophage immunoglobulinlike receptor 10, leukocyte immunoglobulin-like receptor subfamily B member 2, leukocyte immunoglobulin-like receptor subfamily B member 2 soluble isoform 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
GTIPKPTLWA EPDSVITQGS PVTLSCQGSL EAQEYRLYRE KKSASWITRI RPELVKNGQF HIPSITWEHT GRYGCQYYSR ARWSELSDPL VLVMTGAYPK PTLSAQPSPV VTSGGRVTLQ CESQVAFGGF ILCKEGEDEH PQCLNSQPHA RGSSRAIFSV GPVSPNRRWS HRCYGYDLNS PYVWSSPSDL LELLVPGVSK KPSLSVQPGP VMAPGESLTL QCVSDVGYDR FVLYKEGERD LRQLPGRQPQ AGLSQANFTL GPVSRSYGGQ YRCYGAHNLS SECSAPSDPL DILITGQIRG TPFISVQPGP TVASGENVTL LCQSWRQFHT FLLTKAGAAD APLRLRSIHE YPKYQAEFPM SPVTSAHAGT YRCYGSLNSD PYLLSHPSEP LELVVSGPSM GSSPPPTGPI STPAGPEDQP LTPTGSDPQS GLGRHLGVHH HHHH

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

Description:

Mouse Anti Human Dickkopf-Related Protein 3

Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.

Product # :

ANT-707

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Formulation

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

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Introduction
Dickkopf-related protein 3 (DKK3) belongs to the DKK protein family including Dkk-1, 2, 3 and -4. DKK3 is a 350 amino acid secreted glycoprotein which is comprised of an N-terminal signal peptide and 2 conserved cysteine-rich domains that are separated by a 12 amino acid linker region. DKK3 is involved in embryonic development through its inhibition of the WNT signaling pathway. DKK3 gene expression is decreased in a variety of cancer cell lines and it may act as a tumor suppressor gene.
Synonyms
Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human DKK3 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human DKK3 protein (22-350 amino acids purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
PAT103B5AT.
Applications
DKK3 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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
DKK3 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:

Follistatin Human Recombinant

FST, FS

Product # :

CYT-232

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Quantity :

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Description

Follistatin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids and having a total molecular mass of 31.5kDa.The FST is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing no additives.

Purity

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

Biological Activity

The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.

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Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin functions as an ACTV antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
Synonyms
FST, FS
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Follistatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FST 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 Follistatin 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 Gly-Asn-Cys-Trp-Leu.
Background
What is the molecular weight/Mw of FOLLISTATIN HUMAN Protein?
FOLLISTATIN HUMAN Protein has a total Mw of 31.5kDa.

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

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

What is the Biological Activity of FOLLISTATIN HUMAN Protein?
The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.

What is the amino acid sequence of FOLLISTATIN HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.

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

What is the endotoxin level for FOLLISTATIN HUMAN Protein?
The endotoxin level is minimal, FOLLISTATIN 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 Migration Inhibitor Factor Human Recombinant, GST tag

Macrophage Migration Inhibitory Factor (Glycosylation-Inhibiting Factor), Phenylpyruvate Tautomerase, L-Dopachrome Tautomerase, L-Dopachrome Isomerase, GLIF, MMIF, GIF, Macrophage Migration Inhibitory Factor, Glycosylation-Inhibiting Factor, EC 5.3.3.12, EC 5.3.2.1, Macrophage migration inhibitory factor.

Product # :

CYT-401

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Shipped with Ice Packs

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Description

MIF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 345 amino acids (1-115 a.a) and having a molecular mass of 39.2kDa. MIF is fused to a 230 amino acid GST-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MIF protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
Synonyms
Macrophage Migration Inhibitory Factor (Glycosylation-Inhibiting Factor), Phenylpyruvate Tautomerase, L-Dopachrome Tautomerase, L-Dopachrome Isomerase, GLIF, MMIF, GIF, Macrophage Migration Inhibitory Factor, Glycosylation-Inhibiting Factor, EC 5.3.3.12, EC 5.3.2.1, Macrophage migration inhibitory factor.
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
MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPRGSPEFA MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA.

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:

Indoleamine 2,3-Dioxygenase 1 Human Recombinant

IDO, IDO-1, INDO, Indoleamine 2,3-dioxygenase 1, Indoleamine-pyrrole 2,3-dioxygenase.

Product # :

ENZ-807

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Description

IDO1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 426 amino acids (1-403a.a) and having a molecular mass of 47.7kDa. IDO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IDO1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Indoleamine 2,3-Dioxygenase 1 (IDO1) catalyzes the primary and rate-limiting stage in tryptophan catabolism to N-formyl-kynurenine. IDO1 affects on various tryptophan substrates including D-tryptophan, and serotonin and is expressed in dendritic cells, monocytes, and macrophages. IDO1 takes part in a range of pathophysiological processes like neuropathology, antimicrobial and antitumor defense, immunoregulation, and antioxidant activity. IDO1 regulates T-cell behavior by its pericellular catabolization of the necessary amino acid tryptophan.
Synonyms
IDO, IDO-1, INDO, Indoleamine 2,3-dioxygenase 1, Indoleamine-pyrrole 2,3-dioxygenase.
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 MGSMAHAMEN SWTISKEYHI DEEVGFALPN PQENLPDFYN DWMFIAKHLP DLIESGQLRE RVEKLNMLSI DHLTDHKSQR LARLVLGCIT MAYVWGKGHG DVRKVLPRNI AVPYCQLSKK LELPPILVYA DCVLANWKKK DPNKPLTYEN MDVLFSFRDG DCSKGFFLVS LLVEIAAASA IKVIPTVFKA MQMQERDTLL KALLEIASCL EKALQVFHQI HDHVNPKAFF SVLRIYLSGW KGNPQLSDGL VYEGFWEDPK EFAGGSAGQS SVFQCFDVLL GIQQTAGGGH AAQFLQDMRR YMPPAHRNFL CSLESNPSVR EFVLSKGDAG LREAYDACVK ALVSLRSYHL QIVTKYILIP ASQQPKENKT SEDPSKLEAK GTGGTDLMNF LKTVRSTTEK SLLKEG.

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:

Ig gamma-2A chain C region Mouse Recombinant

Immunoglobulin heavy chain constant region gamma 2a, Immunoglobulin G, Ig gamma-2A chain C region, A allele, Ighg.

Product # :

PRO-2842

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Description

IGHG2A Mouse Recombinant produced inSf9 Baculovirus cells is a single glycosylated polypeptide chain containing 242 amino acids (98-330 a.a.) and having a molecular mass of 27.5 kDa. IGHG2A Mouse is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IGHG2A protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Synonyms
Immunoglobulin heavy chain constant region gamma 2a, Immunoglobulin G, Ig gamma-2A chain C region, A allele, Ighg.
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
ADPEPRGPTI KPCPPCKCPA PNLLGGPSVF IFPPKIKDVL MISLSPIVTC VVVDVSEDDP DVQISWFVNN VEVHTAQTQT HREDYNSTLR VVSALPIQHQ DWMSGKEFKC KVNNKDLPAP IERTISKPKG SVRAPQVYVL PPPEEEMTKK QVTLTCMVTD FMPEDIYVEW TNNGKTELNY KNTEPVLDSD GSYFMYSKLR VEKKNWVERN SYSCSVVHEG LHNHHTTKSF SRTPGKHHHH HH.
Background
The Ig gamma-2A chain C region is the constant region of the gamma-2A heavy chain in immunoglobulin molecules, particularly in mice. This region is responsible for various effector functions of IgG2a antibodies, such as antibody-dependent cellular cytotoxicity and phagocytosis and is encoded by the Ighg2a gene. The constant region of the gamma-2A chain takes part in various immune response such as regulation of the immune response, antibody-dependent cellular cytotoxicity and phagocytosis.

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:

sFas Receptor Human Recombinant

Tumor necrosis factor receptor superfamily member 6, Apo-1 antigen, Apoptosis-mediating surface antigen FAS, FASLG receptor, CD95, FAS, APT1, FAS1, APO-1, FASTM, ALPS1A, TNFRSF6.

Product # :

CYT-125

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Quantity :

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Shipped at Room temp

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Description

sFas Receptor Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 157 amino acids and having a molecular mass of 17.6kDa.The FAS is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FAS protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

Purity

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

Biological Activity

The ED₅₀ was determined by its ability to inhibit the cytotoxicity of Jurkat cells is between 10-15 µg/ml in the presence of 2ng/ml of hFasL.

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Introduction
Fas and Fas Ligand (FasL) are members of the TNF superfamily and are type I and type II transmembrane proteins, respectively. Binding of FasL to Fas initiates apoptosis in Fas-bearing cells. The apoptosis mechanism involves the recruitment of pro-caspase 8 through an adaptor molecule named FADD followed by processing of the pro-enzyme to active forms. These active caspases subsequently cleave a variety of cellular substrates leading to the eventual cell death. sFasR is able to inhibit FasL-induced apoptosis by acting as a decoy receptor whicht serves as a sink for FasL. The full length Fas Receptor is a 319 a.a type I transmembrane protein, which contains a 157 a.a extracellular domain, a 17 a.a transmembrane domain, and 145 a.a cytoplasmic domain. The mature human Fas ECD shares 55%, 58%, a.a sequence identity with the mouse, rat, Fas, respectively.
Synonyms
Tumor necrosis factor receptor superfamily member 6, Apo-1 antigen, Apoptosis-mediating surface antigen FAS, FASLG receptor, CD95, FAS, APT1, FAS1, APO-1, FASTM, ALPS1A, TNFRSF6.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FAS although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FAS 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 FAS in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MRLSSKSVNA QVTDINSKGL ELRKTVTTVE TQNLEGLHHD GQFCHKPCPP GERKARDCTV NGDEPDCVPC QEGKEYTDKA HFSSKCRRCR LCDEGHGLEV EINCTRTQNT KCRCKPNFFC NSTVCEHCDP CTKCEHGIIK ECTLTSNTKC KEEGSRS.
Background
What is the molecular weight/Mw of FAS Protein?
FAS Protein has a total Mw of 17.6kDa.

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

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

What is the Biological Activity of FAS Protein?
The ED50 was determined by its ability to inhibit the cytotoxicity of Jurkat cells is between 10-15 µg/ml in the presence of 2ng/ml of hFasL.

What is the amino acid sequence of FAS Protein?
MRLSSKSVNA QVTDINSKGL ELRKTVTTVE TQNLEGLHHD GQFCHKPCPP GERKARDCTV NGDEPDCVPC QEGKEYTDKA HFSSKCRRCR LCDEGHGLEV EINCTRTQNT KCRCKPNFFC NSTVCEHCDP CTKCEHGIIK ECTLTSNTKC KEEGSRS.

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

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

Thyroglobulin Human, Biotinylated

Thyroglobulin, TGN, AITD3, TG.

Product # :

PRO-2563

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Description

Human Thyroglobulin is a biotinylated, glycosylated, polypeptide chain having a total molecular mass of 662 kDa (331 kDa per subunit).

Source

Native, Isolated from human thyroid glands.

Formulation

Human Thyroglobulin biotinylated is supplied at a 20mM HEPES buffer pH-7.6, 150mM NaCl and 40% Sucrose (w/v).

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
Thyroglobulin (TG) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. TG is a large globular dimeric glycoprotein with a total molecular weight of 660 kDa, which occupies a key precursor role in the biosynthesis of the thyroid hormones. Approximately 75% of the total protein content of the thyroid follicle consists of TG. The thyroid gland uses the Thyroglobulin in order to produce the thyroid hormones thyroxine (T4) and triiodothyronine (T3). Thyroglobulin is produced by the thyroid epithelial cells (thyrocytes) which form spherical follicles. Thyroglobulin is subsequently secreted and stored in the follicular lumen.
Patients with Hashimoto's thyroiditis or Graves' disease, frequently develop antibodies against Thyroglobulin. Tg-specific antibodies help in the diagnosis of the above diseases, however they also may be present in apparently healthy euthyroid individuals. Blood Thyroglobulin levels can be used as a tumor marker for certain kinds of thyroid cancer, and the may also be elevated in cases of Graves' disease.
Synonyms
Thyroglobulin, TGN, AITD3, TG.
Physical Appearance
Sterile Filtered 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 IgG type human auto antibodies.2. Auto antibodies to thyroglobulin recognize conformation dependent epitopes. 3.Functional Streptavidin based ELISA test (analysis of positive/negative samples.)

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

Description:

Beta Defensin-3 Human Recombinant

HBD3, HBP3, DEFB3, HBD-3, HBP-3, DEFB103.

Product # :

CYT-461

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Description

Beta Defensin-3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 45 amino acids and having a molecular mass of 5161.2 Dalton. The BD-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HBD-3 was lyophilized without additives.

Purity

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

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Introduction
Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.
Synonyms
HBD3, HBP3, DEFB3, HBD-3, HBP-3, DEFB103.
Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
Stability
Lyophilized Beta Defensin-3 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-3 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 Beta Defensin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GIINTLQKYY CRVRGGRCAV LSCLPKEEQI GKCSTRGRKC CRRKK.
Background
Beta Defensin-3 Human Recombinant: Advancements in Antimicrobial Peptide Therapy
Abstract:

Beta Defensin-3 (hBD-3) human recombinant is a promising antimicrobial peptide with broad-spectrum activity against bacteria, viruses, and fungi. This research paper provides an overview of hBD-3, including its properties, mode of action, and potential applications. Additionally, novel methodologies for the production and optimization of hBD-3 human recombinant are discussed, highlighting its future implications in the field of infectious disease management.
Introduction:

The rise of drug-resistant pathogens necessitates exploring alternative therapeutic approaches, such as antimicrobial peptides. Beta Defensin-3 (hBD-3) human recombinant has emerged as a potent candidate due to its broad-spectrum antimicrobial activity. This paper aims to examine the unique features of hBD-3 and propose innovative methodologies for its production and optimization.
Properties and Mode of Action:

hBD-3 possesses a distinct structural composition consisting of 45 amino acids, including an N-terminal loop, three antiparallel β-strands, and a C-terminal α-helix. These structural elements contribute to its ability to disrupt microbial membranes and target selectivity. The mode of action involves electrostatic interactions with negatively charged microbial membranes, leading to membrane disruption and subsequent cell death. Furthermore, hBD-3 exhibits immunomodulatory functions by promoting chemotaxis, enhancing phagocytic activity, and modulating the release of pro-inflammatory cytokines.
Production of hBD-3 Human Recombinant:

Various expression systems, such as bacterial, yeast, and mammalian cell-based platforms, have been explored for the efficient production of hBD-3 human recombinant. Each system offers distinct advantages and challenges, requiring careful selection to achieve high yields and desired protein quality. Optimization strategies, including codon optimization, fusion protein tags, and appropriate growth conditions, have been employed to enhance production efficiency. Purification techniques, such as chromatography and ultrafiltration, have been optimized to isolate high-quality hBD-3 recombinant.
Applications and Future Perspectives:

hBD-3 human recombinant exhibits significant therapeutic potential against drug-resistant pathogens, making it a promising alternative to conventional antibiotics. It also demonstrates promise in wound healing and tissue regeneration by stimulating angiogenesis, extracellular matrix production, and keratinocyte migration. Moreover, the unique physicochemical properties of hBD-3 open avenues for its utilization in nanomedicine, enabling targeted therapy and improved drug delivery.
Conclusion:

hBD-3 human recombinant represents a potent antimicrobial peptide with broad-spectrum activity against diverse pathogens. The optimization of production methodologies and further exploration of its mechanisms of action will contribute to its clinical utility. With its potential applications in infectious disease management, wound healing, and nanomedicine, hBD-3 human recombinant holds promise as a versatile therapeutic agent.
What is the molecular weight/Mw of BD3 Protein?
BD3 Protein has a total Mw of 5.1kDa.

What is the source or expression system of BD3 Protein?
Escherichia Coli.

What is the Purity of BD3 Protein?
BD3 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BD3 Protein?
The biological functionality of BD3 Protein will be determined in the future.

What is the amino acid sequence of BD3 Protein?
GIINTLQKYY CRVRGGRCAV LSCLPKEEQI GKCSTRGRKC CRRKK.

What applications can BD3 Protein be used in?
BD3 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD3 Protein?
The endotoxin level is minimal, BD3 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:

Adiponectin Human Recombinant, Sf9

Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.

Product # :

CYT-1002

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Description

Acrp30 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 146 amino acids (106-242a.a.) and having a molecular mass of 16.9kDa. (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa). Acrp30 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

Acrp30 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules.
Synonyms
Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.
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
ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16.9kDa.

What is the source or expression system of ADIPONECTIN Protein?
Sf9, Baculovirus cells.

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

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

What is the amino acid sequence of ADIPONECTIN Protein?
ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.

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

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

Immunoglobulin Superfamily Member 8 Human Recombinant

Immunoglobulin Superfamily Member 8, Keratinocytes-Associated Transmembrane Protein 4, Glu-Trp-Ile EWI Motif-Containing Protein 2, Prostaglandin Regulatory-Like Protein, CD81 Partner 3, CD81P3, LIR-D1, EWI-2, KCT-4, EWI2, PGRL, Immunoglobulin Superfamily Member 8, CD316 Antigen, CD316, IgSF8, KCT4.

Product # :

PRO-2451

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Description

IGSF8 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 561 amino acids (28-579a.a.) and having a molecular mass of 59.6kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). IGSF8 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IGSF8 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 30% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Immunoglobulin superfamily member 8 (IGSF8) belongs to the immunoglobulin protein superfamily. IGSF8 interacts with the tetraspanins CD81 and CD9 and may regulate their role in a number of cellular functions including cell migration and viral infection. In addition, the IGSF8 protein may function as a tumor suppressor by inhibiting the proliferation of certain cancers.
Synonyms
Immunoglobulin Superfamily Member 8, Keratinocytes-Associated Transmembrane Protein 4, Glu-Trp-Ile EWI Motif-Containing Protein 2, Prostaglandin Regulatory-Like Protein, CD81 Partner 3, CD81P3, LIR-D1, EWI-2, KCT-4, EWI2, PGRL, Immunoglobulin Superfamily Member 8, CD316 Antigen, CD316, IgSF8, KCT4.
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
ADLREVLVPE GPLYRVAGTA VSISCNVTGY EGPAQQNFEW FLYRPEAPDT ALGIVSTKDT QFSYAVFKSR VVAGEVQVQR LQGDAVVLKI ARLQAQDAGI YECHTPSTDT RYLGSYSGKV ELRVLPDVLQ VSAAPPGPRG RQAPTSPPRM TVHEGQELAL GCLARTSTQK HTHLAVSFGR SVPEAPVGRS TLQEVVGIRS DLAVEAGAPY AERLAAGELR LGKEGTDRYR MVVGGAQAGD AGTYHCTAAE WIQDPDGSWA QIAEKRAVLA HVDVQTLSSQ LAVTVGPGER RIGPGEPLEL LCNVSGALPP AGRHAAYSVG WEMAPAGAPG PGRLVAQLDT EGVGSLGPGY EGRHIAMEKV ASRTYRLRLE AARPGDAGTY RCLAKAYVRG SGTRLREAAS ARSRPLPVHV REEGVVLEAV AWLAGGTVYR GETASLLCNI SVRGGPPGLR LAASWWVERP EDGELSSVPA QLVGGVGQDG VAELGVRPGG GPVSVELVGP RSHRLRLHSL GPEDEGVYHC APSAWVQHAD YSWYQAGSAR SGPVTVYPYM HALDTHHHHH 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:

Endoglin Human Recombinant, His-Tag

CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.

Product # :

CYT-823

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Description

Endoglin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 594 amino acids (26-586) and having a molecular mass of 64.9 kDa. Endoglin is fused to a 36 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

The Endoglin solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 150mM NaCl and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.The Endoglin protein consists of a homodimer of 180 kDA with disulfide links. Endoglin has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Endoglin has been found to be part of the TGF-beta1 receptor complex. Endoglin thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Endoglin expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.
Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSETVH CDLQPVGPER DEVTYTTSQV SKGCVAQAPN AILEVHVLFL EFPTGPSQLE LTLQASKQNG TWPREVLLVL SVNSSVFLHL QALGIPLHLA YNSSLVTFQE PPGVNTTELP SFPKTQILEW AAERGPITSA AELNDPQSIL LRLGQAQGSL SFCMLEASQD MGRTLEWRPR TPALVRGCHL EGVAGHKEAH ILRVLPGHSA GPRTVTVKVE LSCAPGDLDA VLILQGPPYV SWLIDANHNM QIWTTGEYSF KIFPEKNIRG FKLPDTPQGL LGEARMLNAS IVASFVELPL ASIVSLHASS CGGRLQTSPA PIQTTPPKDT CSPELLMSLI QTKCADDAMT LVLKKELVAH LKCTITGLTF WDPSCEAEDR GDKFVLRSAY SSCGMQVSAS MISNEAVVNI LSSSSPQRKK VHCLNMDSLS FQLGLYLSPH FLQASNTIEP GQQSFVQVRV SPSVSEFLLQ LDSCHLDLGP EGGTVELIQG RAAKGNCVSL LSPSPEGDPR FSFLLHFYTV PIPKTGTLSC TVALRPKTGS QDQEVHRTVF MRLNIISPDL SGCTSKG
Background
What is the molecular weight/Mw of CD105 Protein?
CD105 Protein has a total Mw of 64.9kDa.

What is the source or expression system of CD105 Protein?
Escherichia Coli.

What is the Purity of CD105 Protein?
CD105 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of CD105 Protein?
The biological functionality of CD105 Protein will be determined in the future.

What is the amino acid sequence of CD105 Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSETVH CDLQPVGPER DEVTYTTSQV SKGCVAQAPN AILEVHVLFL EFPTGPSQLE LTLQASKQNG TWPREVLLVL SVNSSVFLHL QALGIPLHLA YNSSLVTFQE PPGVNTTELP SFPKTQILEW AAERGPITSA AELNDPQSIL LRLGQAQGSL SFCMLEASQD MGRTLEWRPR TPALVRGCHL EGVAGHKEAH ILRVLPGHSA GPRTVTVKVE LSCAPGDLDA VLILQGPPYV SWLIDANHNM QIWTTGEYSF KIFPEKNIRG FKLPDTPQGL LGEARMLNAS IVASFVELPL ASIVSLHASS CGGRLQTSPA PIQTTPPKDT CSPELLMSLI QTKCADDAMT LVLKKELVAH LKCTITGLTF WDPSCEAEDR GDKFVLRSAY SSCGMQVSAS MISNEAVVNI LSSSSPQRKK VHCLNMDSLS FQLGLYLSPH FLQASNTIEP GQQSFVQVRV SPSVSEFLLQ LDSCHLDLGP EGGTVELIQG RAAKGNCVSL LSPSPEGDPR FSFLLHFYTV PIPKTGTLSC TVALRPKTGS QDQEVHRTVF MRLNIISPDL SGCTSKG

What applications can CD105 Protein be used in?
CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD105 Protein?
The endotoxin level is minimal, CD105 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:

Killer Cell Immunoglobulin-Like Receptor, 3 Domains Long Cytoplasmic Tail 2 Human Recombinant, Sf9

Killer Cell Immunoglobulin Like Receptor, Three Ig Domains And Long Cytoplasmic Tail 2, Killer Cell Immunoglobulin-Like Receptor, Three Domains, Long Cytoplasmic Tail, 2, P70 Natural Killer Cell Receptor Clone CL-5, Natural Killer-Associated Transcript 4, CD158 Antigen-Like Family Member K, MHC Class I NK Cell Receptor, P70 NK Receptor CL-5, CD158K, NKAT-4, NKAT4, Killer Cell Immunoglobulin-Like Receptor 3DL2, Killer-Cell Immunoglobulin-Like Receptor, P70 Killer Cell Inhibitory Receptor, Killer Ig Receptor, KIR Antigen 3DL2, CD158k Antigen, KIR-3DL2, NKAT4B, 3DL2, P140.

Product # :

PRO-2466

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Description

KIR3DL2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 561 amino acids (22-340a.a.) and having a molecular mass of 62.2kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). KIR3DL2 is expressed with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

KIR3DL2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Killer Cell Immunoglobulin-Like Receptor, 3 Domains Long Cytoplasmic Tail 2 (KIR3DL2) is a type 1 transmembrane protein of the p70 family of killer cell Ig-like receptors. KIR3DL2 is a receptor on NK cells for HLA-A alleles which Inhibits their activity consequently preventing cell lysis.
Synonyms
Killer Cell Immunoglobulin Like Receptor, Three Ig Domains And Long Cytoplasmic Tail 2, Killer Cell Immunoglobulin-Like Receptor, Three Domains, Long Cytoplasmic Tail, 2, P70 Natural Killer Cell Receptor Clone CL-5, Natural Killer-Associated Transcript 4, CD158 Antigen-Like Family Member K, MHC Class I NK Cell Receptor, P70 NK Receptor CL-5, CD158K, NKAT-4, NKAT4, Killer Cell Immunoglobulin-Like Receptor 3DL2, Killer-Cell Immunoglobulin-Like Receptor, P70 Killer Cell Inhibitory Receptor, Killer Ig Receptor, KIR Antigen 3DL2, CD158k Antigen, KIR-3DL2, NKAT4B, 3DL2, P140.
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
ADPLMGGQDK PFLSARPSTV VPRGGHVALQ CHYRRGFNNF MLYKEDRSHV PIFHGRIFQE SFIMGPVTPA HAGTYRCRGS RPHSLTGWSA PSNPLVIMVT GNHRKPSLLA HPGPLLKSGE TVILQCWSDV MFEHFFLHRE GISEDPSRLV GQIHDGVSKA NFSIGPLMPV LAGTYRCYGS VPHSPYQLSA PSDPLDIVIT GLYEKPSLSA QPGPTVQAGE NVTLSCSSWS SYDIYHLSRE GEAHERRLRA VPKVNRTFQA DFPLGPATHG GTYRCFGSFR ALPCVWSNSS DPLLVSVTGN PSSSWPSPTE PSSKSGICRH LHVEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH 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:

Serum Amyloid A4 Human Recombinant

Serum amyloid A-4 protein, Constitutively expressed serum amyloid A protein, C-SAA, SAA4, CSAA.

Product # :

CYT-002

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Description

SAA4 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 131 amino acids (21-130 a.a.) and having a molecular mass of 14.9kDa. The SAA4 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SAA4 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 5mM DTT, 0.2M NaCl and 0.5mM EDTA.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
SAA4 is a constitutively expressed protein which is a member of the SAA family. SAA4 is a major acute phase reactant and an apolipoprotein of the HDL complex. SAA4 is constitutively expressed only in humans and mice; it is connected almost completely with lipoproteins of the high density range. The physiological function of SAA4 is unknown, and its serum concentration has no association with those of other major apolipoproteins. SAA4 mRNA and protein occurrence in macrophage derived foam cells of coronary and carotid arteries implied a specific role of human SAA4 during inflammation including atherosclerosis.
Synonyms
Serum amyloid A-4 protein, Constitutively expressed serum amyloid A protein, C-SAA, SAA4, CSAA.
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 MWRSFFKEAL QGVGDMGRAY WDIMISNHQN SNRYLYARGN YDAAQRGPGG VWAAKLISRS RVYLQGLIDY YLFGNSSTVL EDSKSNEKAE EWGRSGKDPD RFRPDGLPKK Y.

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:

Tumor Necrosis Factor Receptor 13B Human Recombinant

CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.

Product # :

CYT-819

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Description

TACI Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids and having a molecular mass of 18.0kDa.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

Fully biologically active when compared to standard. The biological activity is determined by its ability to block human BAFF induced T2B cell survival using a concentration range of 1.0-3.0 µg/ml corresponding to a specific activity of 334-1000 IU/mg.

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Introduction
TNFRSF13B (TACI) is a transmembrane receptor protein found predominantly on the surface of B cells (a significant part of the immune system). TACI was at first discovered owing to its ability to interact with calcium-modulator and cyclophilin ligand (CAML). Later on, it was found that TACI plays a key role in humoral immunity by interacting with two members of the TNF family. Also, TACI controls T cell-independent B cell antibody responses, isotype switching, and B cell homeostasis.
Synonyms
CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TACI although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TACI 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 TACI in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSGLGRSRRG GRSRVDQEER FPQGLWTGVA MRSCPEEQYW DPLLGTCMSC KTICNHQSQR TCAAFCRSLS CRKEQGKFYD HLLRDCISCA SICGQHPKQC AYFCENKLRS PVNLPPELRR QRSGEVENNS DNSGRYQGLE HRGSEASPAL PGLKLSADQV

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:

Integrin Beta 1 Binding Protein 3 Human Recombinant

Nicotinamide riboside kinase 2, Ribosylnicotinamide kinase 2, Ribosylnicotinic acid kinase 2, ITGB1BP3, MIBP, NRK2, NmR-K 2.

Product # :

PRO-1177

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Description

ITGB1BP3 Human Recombinant produced in E. coli is a single polypeptide chain containing 253 amino acids (1-230) and having a molecular mass of 28.4 kDa.ITGB1BP3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ITGB1BP3 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 40% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Nicotinamide riboside kinase 2 (ITGB1BP3) is a member of the uridine kinase family and NRK subfamily. ITGB1BP3 catalyzes the phosphorylation of nicotinic acid riboside and nicotinamide riboside to create nicotinic acid mononucleotide and nicotinamide mononucleotide. ITGB1BP3 reduces laminin matrix deposition and cell adhesion to laminin, but not to fibronectin. ITGB1BP3 is involved in the regulation of PXN at the protein level and of PXN tyrosine phosphorylation. ITGB1BP3 also has a role in the regulation of terminal myogenesis.
Synonyms
Nicotinamide riboside kinase 2, Ribosylnicotinamide kinase 2, Ribosylnicotinic acid kinase 2, ITGB1BP3, MIBP, NRK2, NmR-K 2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMKLIVGI GGMTNGGKTT LTNSLLRALP NCCVIHQDDF FKPQDQIAVG EDGFKQWDVL ESLDMEAMLD TVQAWLSSPQ KFARAHGVSV QPEASDTHIL LLEGFLLYSY KPLVDLYSRR YFLTVPYEEC KWRRSTRNYT VPDPPGLFDG HVWPMYQKYR QEMEANGVEV VYLDGMKSRE ELFREVLEDI QNSLLNRSQE SAPSPARPAR TQGPGRGCGH RTARPAASQQ DSM

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 Factor-4 Variant 1 Human Recombinant

CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

Product # :

CHM-243

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Description

CXCL4 Variant-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa. The CXCL4 Variant-1 is fused to 6xHis tag at N-Terminus and purified by standard chromatography techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized in PBS, pH 8.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Platelet factor-4 is a 70-amino acid protein that is
released from the alpha-granules of activated platelets. Its major physiologic
role appears to be neutralization of molecules on the endothelial surface of
blood vessels, thereby inhibiting local antithrombin III activity and promoting
coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4
probably has a role in inflammation and wound repair. Oncostatin-A is a member
of the CXC chemokine family. Furthermore it is used as an inhibitor in the
angiogenesis during tumor therapy.
Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Human CXCL4 although stable at 25°C 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CXCL4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MHHHHHHEAE EDGDLQCLCV KTTSQVRPRH ITSLEVIKAG PHCPTAQLIA TLKNGRKICL DLQALLYKKI IKEHLES.
Background
What is the molecular weight/Mw of CXCL4 VARIANT 1 HUMAN Protein?
CXCL4 VARIANT 1 HUMAN Protein has a total Mw of 8.7kDa.

What is the source or expression system of CXCL4 VARIANT 1 HUMAN Protein?
Escherichia Coli.

What is the Purity of CXCL4 VARIANT 1 HUMAN Protein?
CXCL4 VARIANT 1 HUMAN Protein is > 95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL4 VARIANT 1 HUMAN Protein?
The biological functionality of CXCL4 VARIANT 1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of CXCL4 VARIANT 1 HUMAN Protein?
MHHHHHHEAE EDGDLQCLCV KTTSQVRPRH ITSLEVIKAG PHCPTAQLIA TLKNGRKICL DLQALLYKKI IKEHLES.

What applications can CXCL4 VARIANT 1 HUMAN Protein be used in?
CXCL4 VARIANT 1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL4 VARIANT 1 HUMAN Protein?
The endotoxin level is minimal, CXCL4 VARIANT 1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL4 VARIANT 1 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 CXCL4 VARIANT 1 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:

Allergen Ara h 8.0101 Recombinant

Ara h 8 allergen.

Product # :

ALR-010

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Description

Recombinant Ara h 8.0101 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 18,192 Dalton. Ara h 8.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Sf9 insect cells.

Formulation

Ara h 8.0101 is supplied in 20mM HEPES buffer pH-8, 0.1M NaCl and 6M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Ara h 8.0101 which is a part of the PR-10 protein family is a Bet v 1-homologous panallergen. Ara h 8.0101 is cross-reactive with Gly m 4 from soy bean and Bet v 1 from silver birch. Ara h 8.0101 is responsible for oral allergy syndrome and also has low stability to roasting and no stability to gastric digestion.
Synonyms
Ara h 8 allergen.
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.

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:

Trefoil Factor-3 Human Recombinant

TFF-3, ITF, TFI, HITF, hP1.B, TFF3, Trefoil factor 3, Intestinal trefoil factor.

Product # :

CYT-005

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Description

TFF-3 Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 59 amino acid chains which includes a 40 amino acid trefoil motif containing 3 conserved interamolecular disulfide bonds and having a total molecular mass of 13.2kDa. TFF-3 Human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

The ED50 as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10µg/ml, corresponding to a specific activity of > 100IU/mg.

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Introduction
Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains. TFF3 induces ciliogenesis and promotes airway epithelial ciliated cell differentiation, relatively through an epidermal growth factor receptor-dependent pathway. TFF3 overexpression is crucial for progression in mouse and human hepatocellular carcinogenesis. TFF-3 is normally expressed in hepatocellular carcinoma and its expression associates with tumor grade.
Synonyms
TFF-3, ITF, TFI, HITF, hP1.B, TFF3, Trefoil factor 3, Intestinal trefoil factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TFF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF3 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 TFF3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
EEYVGLSANQ CAVPAKDRVD CGYPHVTPKE CNNRGCCFDS RIPGVPWCFK PLQEAECTF.

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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