Search: 1000 results found for "avidin"

Description:

Vacuolar Protein Sorting 26A Human Recombinant

Vacuolar protein sorting-associated protein 26A, Vesicle protein sorting 26A, hVPS26, VPS26A, VPS26, HB58, PEP8A, Hbeta58.

Product # :

PRO-1161

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Description

VPS26A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-327 a.a) and having a molecular mass of 40.6kDa.VPS26A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

VPS26A protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.15M NaCl.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Vacuolar protein sorting-associated protein 26A (VPS26A) is a vital element of the retromer complex, which is required to recover lysosomal enzyme receptors (IGF2R and M6PR) from endosomes to the trans-Golgi network. Furthermore, VPS26A is essential in the regulation of transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Expression analysis in yeast and mammalian cells reveal that VPS26A interacts directly with VPS35 that functions as the core of the retromer complex.
Synonyms
Vacuolar protein sorting-associated protein 26A, Vesicle protein sorting 26A, hVPS26, VPS26A, VPS26, HB58, PEP8A, Hbeta58.
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 MGSMSFLGGF FGPICEIDIV LNDGETRKMA EMKTEDGKVE KHYLFYDGES VSGKVNLAFK QPGKRLEHQG IRIEFVGQIE LFNDKSNTHE FVNLVKELAL PGELTQSRSY DFEFMQVEKP YESYIGANVR LRYFLKVTIV RRLTDLVKEY DLIVHQLATY PDVNNSIKME VGIEDCLHIE FEYNKSKYHL KDVIVGKIYF LLVRIKIQHM ELQLIKKEIT GIGPSTTTET ETIAKYEIMD GAPVKGESIP IRLFLAGYDP TPTMRDVNKK FSVRYFLNLV LVDEEDRRYF KQQEIILWRK APEKLRKQRT NFHQRFESPE SQASAEQPEM.

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 (20-110 a.a) Human Recombinant

Product # :

CYT-1237

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Description

The Insulin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Insulin His-Tagged Fusion Protein, produced in E. coli, is a 13kDa protein containing 91 amino acid residues of the Insulin Human, 20-110 amino acids.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90% as determined by SDS-PAGE.

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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized Insulin at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Amino Acid Sequence
MALWMRLLPL LALLALWGPD PAAAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN
Background
Insulin participates in the metabolism of carbohydrates, proteins and fats by regulating glucose homeostasis in the body. Insulin decreases blood glucose concentration. Insulin hormone facilitates the uptake of glucose into cells, mainly in muscle and fat tissues, and stimulates the liver to store glucose as glycogen. Insulin also inhibits the production of gluconeogenesis and promotes the synthesis of proteins and lipids. Insulin increases cell permeability to monosaccharides, fatty acids and amino acids. Insulin accelerates glycolysis, the pentose phosphate cycle and glycogen synthesis in liver.

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:

Acid Phosphatase Prostate Human Recombinant

PAP, ACP3, ACP-3, Acid phosphatase, prostate, 5'-nucleotidase, 5'-NT, Ecto-5'-nucleotidase, Thiamine monophosphatase, TMPase.

Product # :

ENZ-847

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Description

ACPP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 375 amino acids (33-386 a.a) and having a molecular mass of 43.2kDa.ACPP is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ACPP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Acid phosphatase, prostate (ACPP) is a non-specific tyrosine phosphatase, which dephosphorylates a varied number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. ACPP has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma.
Synonyms
PAP, ACP3, ACP-3, Acid phosphatase, prostate, 5'-nucleotidase, 5'-NT, Ecto-5'-nucleotidase, Thiamine monophosphatase, TMPase.
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 MKELKFVTLV FRHGDRSPID TFPTDPIKES SWPQGFGQLT QLGMEQHYEL GEYIRKRYRK FLNESYKHEQ VYIRSTDVDR TLMSAMTNLA ALVPPEGVSI WNPILLWQPI PVHTVPLSED QLLYLPFRNC PRFQELESET LKSEEFQKRL HPYKDFIATL GKLSGLHGQD LFGIWSKVYD PLYCESVHNF TLPSRATEDT MTKLRELSEL SLLSLYGIHK QKEKSRLQGG VLVNEILNHM KRATQIPSYK KLIMYSAHDT TVSGLQMALD VYNGLLPPYA SCHLTELYFE KGEYFVEMYY RNETQHEPYP LMLPGCSPSC PLERFAELVG PVIPQDWSTE CMTTNSHQGT EDSTD.

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-2 Mouse Recombinant

Beta-defensin 2, BD-2, mBD-2, Defensin beta 2, Defb2, MGC129140, MGC129141.

Product # :

CYT-035

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Description

Beta Defensin-2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 5.5kDa. The BD-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Mouse BD-2 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

Determined by the ability to chemoattract immature human dendritic cells at a concentration of 10-100ng/ml.

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Introduction
The Defensin family are highly similar in their protein sequence and are microbicidal & cytotoxic peptides made by neutrophils. Beta Defensin-1 is an antimicrobial peptide having the resistance of epithelial surfaces to microbial colonization. Beta Defensin-1 has close proximity to Defensin Alpha-1 and has been implicated in the pathogenesis of cystic fibrosis.
Skin of patients having atopic dermatitis patients and mycosis fungoides (non-lesional and lesional) show lower human Beta Defensin-1 mRNA expression and higher human Beta Defensin-2 and human Beta Defensin-3 mRNA expression.
BBeta Defensin is highly expressed by epithelial cells.
Beta-defensin 1 may play a role in the pathogenesis of severe sepsis.
Variation in human Beta Defensin-1 contributes to asthma diagnosis, with apparent gender-specific effects. Human Beta Defensin-3 is a dimer, while Human BD-1 and Human BD-2 are monomeric. The expression of Human BD1 is correlated with induction profiles in gingival keratinocytes.
The level of expression of human DEFB1 mRNA is lower than that of human BD3 and human BD-2 in reconstructed epidermis.
Human BD1 is down-regulated in human prostatic and renal carcinomas.
Synonyms
Beta-defensin 2, BD-2, mBD-2, Defensin beta 2, Defb2, MGC129140, MGC129141.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Beta Defensin-2 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-2 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-2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AVGSLKSIGY EAELDHCHTN GGYCVRAICP PSARRPGSCF PEKNPCCKYM K.
Background
What is the molecular weight/Mw of BD2 Protein?
BD2 Protein has a total Mw of 5.5kDa.

What is the source or expression system of BD2 Protein?
Escherichia Coli.

What is the Purity of BD2 Protein?
BD2 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of BD2 Protein?
Determined by the ability to chemoattract immature human dendritic cells at a concentration of 10-100ng/ml.

What is the amino acid sequence of BD2 Protein?
AVGSLKSIGY EAELDHCHTN GGYCVRAICP PSARRPGSCF PEKNPCCKYM K.

What applications can BD2 Protein be used in?
BD2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD2 Protein?
The endotoxin level is minimal, BD2 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 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:

Vaspin, Mouse Anti Human

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

Product # :

ANT-366

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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
Vaspin (visceral adipose-specific SERPIN), a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.
Synonyms
Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.
Immunogen
Anti-human Vaspin mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human Vaspin amino acids 21-414 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
P1C4AT.
Applications
Vaspin antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000 ~ 3,000. Recommended starting dilution is 1:2,000.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
Vaspin antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

Description:

Aspartylglucosaminidase Human Recombinant, sf9

Aspartylglucosaminidase, Glycosylasparaginase, N4-(N-Acetyl-Beta-Glucosaminyl)-L-Asparagine Amidase, N(4)-(Beta-N-Acetylglucosaminyl)-L-Asparaginase , EC 3.5.1.26, Aspartylglucosylamine Deaspartylase, EC 3.5.1, ASRG, AGU, GA.

Product # :

ENZ-990

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Description

AGA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 332 amino acids (24-346 a.a.) and having a molecular mass of 35.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-57kDa). AGA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

AGA protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Aspartylglucosaminidase, also known as AGA, takes part in the catabolism of Nlinked oligosaccharides of glycoproteins. AGA is a protein coding gene which cleaves asparagine from N-acetylglucosamines in the lysosomal breakdown of glycoproteins.
Synonyms
Aspartylglucosaminidase, Glycosylasparaginase, N4-(N-Acetyl-Beta-Glucosaminyl)-L-Asparagine Amidase, N(4)-(Beta-N-Acetylglucosaminyl)-L-Asparaginase , EC 3.5.1.26, Aspartylglucosylamine Deaspartylase, EC 3.5.1, ASRG, AGU, GA.
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
ADPSSPLPLV VNTWPFKNAT EAAWRALASG GSALDAVESG CAMCEREQCD GSVGFGGSPD ELGETTLDAM IMDGTTMDVG AVGDLRRIKN AIGVARKVLE HTTHTLLVGE SATTFAQSMG FINEDLSTTA SQALHSDWLA RNCQPNYWRN VIPDPSKYCG PYKPPGILKQ DIPIHKETED DRGHDTIGMV VIHKTGHIAA GTSTNGIKFK IHGRVGDSPI PGAGAYADDT AGAAAATGNG DILMRFLPSY QAVEYMRRGE DPTIACQKVI SRIQKHFPEF FGAVICANVT GSYGAACNKL STFTQFSFMV YNSEKNQPTE EKVDCIHHHH HH.

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:

Inositol Monophosphatase Domain Containing 1 Mouse Recombinant Bioactive

Inositol monophosphatase 3, IMP 3, IMPase 3, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3.

Product # :

PRO-2380

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Description

IMPAD1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 332 amino acids (34-356a.a.) and having a molecular mass of 36.2kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). IMPAD1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IMPAD1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 5,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze Adenosine 3, 5-diphosphate per minute at pH 7.5 at 25C.

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Introduction
Inositol monophosphatase 3 (IMPAD1) belongs to the inositol monophosphatase family. IMPAD1 is restricted to the Golgi apparatus and catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to adenosine monophosphate (AMP). IMPAD1 gene mutations cause the GRAPP type chondrodysplasia with joint dislocations, and a pseudogene of the IMPAD1 gene is located on the long arm of chromosome 1.
Synonyms
Inositol monophosphatase 3, IMP 3, IMPase 3, Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase, Golgi-resident PAP phosphatase, gPAPP, Inositol monophosphatase domain-containing protein 1, Inositol-1(or 4)-monophosphatase 3, Myo-inositol monophosphatase A3.
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
ADPGRFSLFG LGSEPAAGEA EVASDGGTVD LREMLAVAVL AAERGGDEVR RVRESNVLHE KSKGKTREGA DDKMTSGDVL SNRKMFYLLK TAFPNVQINT EEHVDASDKE VIVWNRKIPE DILKEIAAPK EVPAESVTVW IDPLDATQEY TEDLRKYVTT MVCVAVNGKP VLGVIHKPFS EYTAWAMVDG GSNVKARSSY NEKTPKIIVS RSHAGMVKQV ALQTFGNQTS IIPAGGAGYK VLALLDVPDM TQEKADLYIH VTYIKKWDIC AGNAILKALG GHMTTLNGEE ISYTGSDGIE GGLLASIRMN HQALVRKLPD LEKSGHHHHH HH.

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:

Coiled-Coil Domain Containing 69 Human Recombinant

Coiled-coil domain-containing protein 69, CCDC69.

Product # :

PRO-1880

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Description

CCDC69 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 319 amino acids (1-296 a.a) and having a molecular mass of 37.2kDa. CCDC69 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CCDC69 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Coiled-Coil Domain Containing 69, also known as CCDC69 is a protein-coding gene. A significant paralog of CCDC69 is MTUS1.
Synonyms
Coiled-coil domain-containing protein 69, CCDC69.
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 MGSMGCRHSR LSSCKPPKKK RQEPEPEQPP RPEPHELGPL NGDTAITVQL CASEEAERHQ KDITRILQQH EEEKKKWAQQ VEKERELELR DRLDEQQRVL EGKNEEALQV LRASYEQEKE ALTHSFREAS STQQETIDRL TSQLEAFQAK MKRVEESILS RNYKKHIQDY GSPSQFWEQE LESLHFVIEM KNERIHELDR RLILMETVKE KNLILEEKIT TLQQENEDLH VRSRNQVVLS RQLSEDLLLT REALEKEVQL RRQLQQEKEE LLYRVLGANA SPAFPLAPVT PTEVSFLAT.

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

Description:

Leptin N82K Human Recombinant, Pegylated

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-1107

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Description

Pegylated Leptin N82K Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Pegylated Leptin N82K Human Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3 Having 35-40% protein.

Purity

Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.

Biological Activity

Pegylated Leptin Human is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated Leptin in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo Pegylated Leptin has profound weight reducing effect (as compared to the non-pegylated recombinant human leptin), resulting mainly from reduced food intake.

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Introduction
Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Pegylated Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pegylated Leptin N82K 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 Pegylated Leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

Description:

Leptin Salamander Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor, Leptin.

Product # :

CYT-704

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Quantity :

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Description

Leptin Salamander Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of 16kDa. The Salamander Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Salamander Leptin was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

Purity

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

Biological Activity

By inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its activity in that test is similar to that of mouse leptin.

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized recombinant salamander leptin although stable at room temperature for several weeks, should be stored desiccated below -18C. Upon reconstitution of recombinant salamander leptin at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization recombinant salamander leptin can be stored at +4C for at least two weeks.
Solubility
It is recommended to reconstitute the lyophilized Salamander Leptin in sterile 0.4% NaHCO3 pH-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the ten N-terminal amino acids was determined and was found to be Ala-Ile-Met-Val-Asp-Gln-Leu-Arg-Met-Asp.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.104 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

Description:

Leptin Antagonist Triple Mutant Human Recombinant

Product # :

CYT-352

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Description

Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A. Leptin Antagonist Triple Mutant Human Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

Purity

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

Biological Activity

ProSpec’s Leptin triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

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Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin Antagonist Triple Mutant Human Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Human Recombinant in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

Description:

Interferon Alpha and Beta Receptor Subunit 1 Human Recombinant

IFN-alpha/beta R1, IFNAR1, AVP, IFN-alpha-REC, IFNAR, IFNBR, IFRC, Interferon alpha/beta receptor 1, IFN-R-1, IFN-alpha/beta receptor 1, Cytokine receptor class-II member 1, Cytokine receptor family 2 member 1, CRF2-1, Type I interferon receptor 1.

Product # :

CYT-1138

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Description

IFNAR1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 415 amino acids (28-436a.a.) and having a molecular mass of 47.9kDa. IFNAR1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

IFNAR1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Interferon Alpha And Beta Receptor or IFNAR1, is part of the class II cytokine receptor family. IFNAR1 forms one of the two chains of a receptor for interferons alpha and beta. IFNAR1 binds and activates the receptor that stimulates Janus protein kinases, which then phosphorylate few proteins, including STAT1 & STAT2. Furthermore, IFNAR1 also acts as an antiviral factor.
Synonyms
IFN-alpha/beta R1, IFNAR1, AVP, IFN-alpha-REC, IFNAR, IFNBR, IFRC, Interferon alpha/beta receptor 1, IFN-R-1, IFN-alpha/beta receptor 1, Cytokine receptor class-II member 1, Cytokine receptor family 2 member 1, CRF2-1, Type I interferon receptor 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
KNLKSPQKVE VDIIDDNFIL RWNRSDESVG NVTFSFDYQK TGMDNWIKLS GCQNITSTKC NFSSLKLNVY EEIKLRIRAE KENTSSWYEV DSFTPFRKAQ IGPPEVHLEA EDKAIVIHIS PGTKDSVMWA LDGLSFTYSL VIWKNSSGVE ERIENIYSRH KIYKLSPETT YCLKVKAALL TSWKIGVYSP VHCIKTTVEN ELPPPENIEV SVQNQNYVLK WDYTYANMTF QVQWLHAFLK RNPGNHLYKW KQIPDCENVK TTQCVFPQNV FQKGIYLLRV QASDGNNTSF WSEEIKFDTE IQAFLLPPVF NIRSLSDSFH IYIGAPKQSG NTPVIQDYPL IYEIIFWENT SNAERKIIEK KTDVTVPNLK PLTVYCVKAR AHTMDEKLNK SSVFSDAVCE KTKPGNTSKH HHHHH.
Background
What is the molecular weight/Mw of IFNAR1 HUMAN Protein?
IFNAR1 HUMAN Protein has a total Mw of 47.9kDa.

What is the source or expression system of IFNAR1 HUMAN Protein?
Sf9, Insect cells.

What is the Purity of IFNAR1 HUMAN Protein?
IFNAR1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNAR1 HUMAN Protein?
The biological functionality of IFNAR1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IFNAR1 HUMAN Protein?
KNLKSPQKVE VDIIDDNFIL RWNRSDESVG NVTFSFDYQK TGMDNWIKLS GCQNITSTKC NFSSLKLNVY EEIKLRIRAE KENTSSWYEV DSFTPFRKAQ IGPPEVHLEA EDKAIVIHIS PGTKDSVMWA LDGLSFTYSL VIWKNSSGVE ERIENIYSRH KIYKLSPETT YCLKVKAALL TSWKIGVYSP VHCIKTTVEN ELPPPENIEV SVQNQNYVLK WDYTYANMTF QVQWLHAFLK RNPGNHLYKW KQIPDCENVK TTQCVFPQNV FQKGIYLLRV QASDGNNTSF WSEEIKFDTE IQAFLLPPVF NIRSLSDSFH IYIGAPKQSG NTPVIQDYPL IYEIIFWENT SNAERKIIEK KTDVTVPNLK PLTVYCVKAR AHTMDEKLNK SSVFSDAVCE KTKPGNTSKH HHHHH.

What applications can IFNAR1 HUMAN Protein be used in?
IFNAR1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNAR1 HUMAN Protein?
The endotoxin level is minimal, IFNAR1 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:

Biotinidase Human Recombinant

Biotinidase, EC 3.5.1.12, Biotinase, EC 3.5.1.

Product # :

ENZ-1004

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Description

BTD Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 510 amino acids (44-545a.a) and having a molecular mass of 57.8kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). BTD is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

BTD protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Biotinidase also known BTD, belongs to the nitrilase superfamily, which contains 12 families of nitrilases, amidases, carbamylases, and N-acyltrasferases. BTD catalyzes the hydrolysis of biocytin, the product of biotin-dependent carboxylase degradation, to biotin and lysine. BTD has a vital regulatory part in chromatin/DNA function. Mutations in BTD protein lead to Biotinidase deficiency.
Synonyms
Biotinidase, EC 3.5.1.12, Biotinase, EC 3.5.1.
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
AHTGEESVAD HHEAEYYVAA VYEHPSILSL NPLALISRQE ALELMNQNLD IYEQQVMTAA QKDVQIIVFP EDGIHGFNFT RTSIYPFLDF MPSPQVVRWN PCLEPHRFND TEVLQRLSCM AIRGDMFLVA NLGTKEPCHS SDPRCPKDGR YQFNTNVVFS NNGTLVDRYR KHNLYFEAAF DVPLKVDLIT FDTPFAGRFG IFTCFDILFF DPAIRVLRDY KVKHVVYPTA WMNQLPLLAA IEIQKAFAVA FGINVLAANV HHPVLGMTGS GIHTPLESFW YHDMENPKSH LIIAQVAKNP VGLIGAENAT GETDPSHSKF LKILSGDPYC EKDAQEVHCD EATKWNVNAP PTFHSEMMYD NFTLVPVWGK EGYLHVCSNG LCCYLLYERP TLSKELYALG VFDGLHTVHG TYYIQVCALV RCGGLGFDTC GQEITEATGI FEFHLWGNFS TSYIFPLFLT SGMTLEVPDQ LGWENDHYFL RKSRLSSGLV TAALYGRLYE RDLEHHHHHH.

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:

Glial-Derived Neurotrophic Factor Human Recombinant, Sf9

Glial cell line-derived neurotrophic factor, hGDNF, Astrocyte-derived trophic factor, ATF, ATF1, ATF2, HFB1-GDNF, HSCR3.

Product # :

CYT-1162

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Description

GDNF Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 113amino acids (109-211 aa) and having a molecular mass of 12.8kDa.GDNF is fused to an 10 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

GDNF protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Glial cell-derived neurotrophic factor or GDNF is part of the GDNF group of ligands proteins. GDNF has a crucial part in numerous cell mechanisms such as neurite outgrowth, cell differentiation, cell survival and migration of cells. GDNF enhances neurons survival via GFRa receptors (mainly GFRa1). The mentioned neurons can die as a result from Parkinson's disease or ALS (amyotrophic lateral sclerosis). This protein takes part in the development of the spermatogenesis & kidney, also, it has a role in alcohol metabolism as ameliorating.
Synonyms
Glial cell line-derived neurotrophic factor, hGDNF, Astrocyte-derived trophic factor, ATF, ATF1, ATF2, HFB1-GDNF, HSCR3.
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
ADPMRGQRGK NRGCVLTAIH LNVTDLGLGY ETKEELIFRY CSGSCDAAET TYDKILKNLS RNRRLVSDKV GQACCRPIAF DDDLSFLDDN LVYHILRKHS AKRCGCIHHH HHH
Background
What is the molecular weight/Mw of GDNF HUMAN, SF9 Protein?
GDNF HUMAN, SF9 Protein has a total Mw of 12.8kDa.

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

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

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

What is the amino acid sequence of GDNF HUMAN, SF9 Protein?
ADPMRGQRGK NRGCVLTAIH LNVTDLGLGY ETKEELIFRY CSGSCDAAET TYDKILKNLS RNRRLVSDKV GQACCRPIAF DDDLSFLDDN LVYHILRKHS AKRCGCIHHH HHH

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

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

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

Description:

Selectin P Ligand Human Recombinant

Cutaneous Lymphocyte-Associated Associated Antigen, Selectin P Ligand, PSGL-1, CD162 Antigen, P-Selectin Glycoprotein Ligand 1, CLA.

Product # :

PRO-2714

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Description

SELPLG Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 496 amino acids (42-295 a.a) and having a molecular mass of 53.4kDa.SELPLG is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The SELPLG solution (1mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
SELPLG glycoprotein functions as a high affinity counter-receptor for the cell adhesion selectin molecules (P, E and L) located in stimulated T lymphocytes and myeloid cells. SELPLG binds leukocytes to activated platelets or endothelia expressing selectins, a vital role in leukocyte trafficking throughout inflammation. In order to have a high-affinity binding activity SELPLG needs two post-translational modifications, tyrosine sulfation and the addition of the sialyl Lewis x tetrasaccharide (sLex) to its O-linked glycans. Polymorphisms and abnormal expression of SELPLG are linked to defects in the innate and adaptive immune response. Alternate splicing results in multiple transcript variants.
Synonyms
Cutaneous Lymphocyte-Associated Associated Antigen, Selectin P Ligand, PSGL-1, CD162 Antigen, P-Selectin Glycoprotein Ligand 1, CLA.
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
DGSQATEYEY LDYDFLPETE PPEMLRNSTD TTPLTGPGTP ESTTVEPAAR RSTGLDAGGA VTELTTELAN MGNLSTDSAA MEIQTTQPAA TEAQTTPLAA TEAQTTRLTA TEAQTTPLAA TEAQTTPPAA TEAQTTQPTG LEAQTTAPAA MEAQTTAPAA MEAQTTPPAA MEAQTTQTTA MEAQTTAPEA TEAQTTQPTA TEAQTTPLAA MEALSTEPSA TEALSMEPTT KRGLFIPFSV SSVTHKGIPM AASNLSVLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH

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

Description:

Calcitonin Acetate Salmon

CT, KC, CGRP, CALC1, CGRP1, CGRP-I, MGC126648, katacalcin, Calcitonin gene-related peptide 1 precursor, Calcitonin gene-related peptide I.

Product # :

HOR-262

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Quantity :

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Description

Calcitonin Acetate (Salmon) is a synthetic polypeptide of 32 amino acids in the same linear sequence that is found in calcitonin of salmon origin. The Molecular Formula is C145H240N44O48S2. Calcitonin Molecular Weight: 3431.9 Dalton.

Formulation

The calcitonin peptide was lyophilized with no additives.

Purity

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

More Info

Introduction
Calcitonin (CT) is a peptide hormone produced by the parafollicular cells of the thyroid gland in mammals and by the ultimobranchial gland of birds and fish. Salmon calcitonin (sCT), which is more potent and longer lasting than human CT, has been used widely for the treatment of osteoporosis, paget's disease, hypercalcemic shock and chronic pain in terminal cancer patients. sCT is one of the many bioactive peptides that require C-terminal amidation for full biological activity.
Synonyms
CT, KC, CGRP, CALC1, CGRP1, CGRP-I, MGC126648, katacalcin, Calcitonin gene-related peptide 1 precursor, Calcitonin gene-related peptide I.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Calcitonin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CGRP 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 Calcitonin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Calcitonin Acetate (Salmon) has an amino acid sequence of: Cys-Ser-Asn-Leu-Ser-Thr-Cys-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Thr-Gly-Ser-Gly-Thr-Pro-NH2.

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:

Epstein Barr Virus Induced 3 Human Recombinant

Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein, EBI3, IL27B.

Product # :

CYT-367

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Quantity :

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Shipped at Room temp

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Description

EBI3 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 209 amino acids fragment (21-229) having a molecular weight of 23.3kDa. The EBI3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EBI3 Human Recombinant was lyophilized from a solution containing 10mM Acetic Acid and 0.5% Mannitol.

Purity

Greater than 90% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Assay data for Human recombinant EBI3 is based upon qualitative binding to anti-EBI3 antibody.

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Introduction
EBI3 has an induced expression in B lymphocytes in reaction to Epstein-Barr virus infection. EBI3 encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form iIL-27. EBI3 drives rapid clonal expansion of naive cd4(+) t-cells. EBI3 strongly synergizes with IL-12 to activate IFN-gamma production of naive cd4(+) t-cells. EBI3 mediates its biologic effects through the cytokine receptor wsx-1/tccr.
Synonyms
Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein, EBI3, IL27B.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EBI3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EBI3 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 EBI3 in sterile 10mM Acetic acid not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
RKGPPAALTLPRVQCRASRYPIAVDCSWTLPPAPNSTSPVSF
IATYRLGMAARGHSWPCLQQTPTSTSCTITDVQLFSMAPYVL
NVTAVHPWGSSSSFVPFITEHIIKPDPPEGVRLSPLAERQLQ
VQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSF
ILRAVRPRARYYVQVAAQDLTDYGELSDWSLPATATMSLGK.
Background
Title: Epstein-Barr Virus Induced 3 Human Recombinant: Unveiling its Role in Epstein-Barr Virus-Associated Diseases
Abstract:

Epstein-Barr Virus Induced 3 (EBI3) is a crucial cytokine involved in the immune response against Epstein-Barr virus (EBV) and various other pathogens. This research paper provides an extensive analysis of human recombinant EBI3, focusing on its production, characterization, and potential applications in understanding EBV-associated diseases. The paper highlights the significance of EBI3 in modulating immune responses and explores its role in the pathogenesis of EBV-related malignancies. Furthermore, it discusses ongoing research and clinical trials investigating the therapeutic potential of recombinant EBI3 in immune disorders and cancer. The information presented in this paper aims to enhance our understanding of human recombinant EBI3 and its utility as a research tool and a potential immunotherapeutic agent.
Introduction:

Epstein-Barr Virus Induced 3 (EBI3) is a cytokine that plays a critical role in the immune response against EBV. Human recombinant EBI3, produced through genetic engineering techniques, provides a valuable tool for studying its immunomodulatory properties and exploring its potential therapeutic applications.
Production and Characterization:

Recombinant EBI3 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant EBI3.
Role in EBV-Associated Diseases:

EBI3 is involved in the regulation of immune responses during EBV infection. It acts as a subunit of the heterodimeric cytokine interleukin-27 (IL-27), which plays a crucial role in anti-viral immunity. Recombinant EBI3 serves as a valuable tool for investigating the mechanisms underlying EBI3-mediated immune regulation and its potential implications in EBV-associated diseases, including infectious mononucleosis, nasopharyngeal carcinoma, and EBV-related lymphomas.
Therapeutic Implications:

Dysregulation of the immune response is implicated in various immune disorders and cancers. Recombinant EBI3 holds promise as a potential immunotherapeutic agent due to its immunomodulatory properties. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant EBI3 in conditions such as autoimmune diseases, viral infections, and cancer.
Conclusion:

Human recombinant EBI3 represents a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in understanding EBV-associated diseases contribute to our understanding of immune regulation and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant EBI3 offer promising avenues for improving outcomes in immune disorders and EBV-related malignancies.
What is the molecular weight/Mw of EBI3 Protein?
EBI3 Protein has a total Mw of 23.3kDa.

What is the source or expression system of EBI3 Protein?
Escherichia Coli.

What is the Purity of EBI3 Protein?
EBI3 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of EBI3 Protein?
Assay data for Human recombinant EBI3 is based upon qualitative binding to anti-EBI3 antibody.

What is the amino acid sequence of EBI3 Protein?
RKGPPAALTLPRVQCRASRYPIAVDCSWTLPPAPNSTSPVSF
IATYRLGMAARGHSWPCLQQTPTSTSCTITDVQLFSMAPYVL
NVTAVHPWGSSSSFVPFITEHIIKPDPPEGVRLSPLAERQLQ
VQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSF
ILRAVRPRARYYVQVAAQDLTDYGELSDWSLPATATMSLGK.

What applications can EBI3 Protein be used in?
EBI3 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EBI3 Protein?
The endotoxin level is minimal, EBI3 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:

Isopentenyl-Diphosphate Delta Isomerase 2 Human Recombinant

Isopentenyl-diphosphate Delta-isomerase 2, Isopentenyl pyrophosphate isomerase 2, IPP isomerase 2, IPPI2, IDI2.

Product # :

ENZ-107

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Quantity :

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Shipped with Ice Packs

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Description

IDI2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 247 amino acids (1-227 a.a.) and having a molecular mass of 28.9kDa.IDI2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IDI2 solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 0.1mM PMSF.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Isopentenyl-diphosphate Delta-isomerase 2 (IDI2) is a member of the IPP isomerase type 1 family. IDI2 catalyzes the 1,3-allylic reorganization of the homoallylic substrate isopentenyl (IPP) to its extremely electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Synonyms
Isopentenyl-diphosphate Delta-isomerase 2, Isopentenyl pyrophosphate isomerase 2, IPP isomerase 2, IPPI2, IDI2.
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 MSDINLDWVD RRQLQRLEEM LIVVDENDKV IGADTKRNCH LNENIEKGLL HRAFSVVLFN TKNRILIQQR SDTKVTFPGY FTDSCSSHPL YNPAELEEKD AIGVRRAAQR RLQAELGIPG EQISPEDIVF MTIYHHKAKS DRIWGEHEIC YLLLVRKNVT LNPDPSETKS ILYLSQEELW ELLEREARGE VKVTPWLRTI AERFLYRWWP HLDDVTPFVE LHKIHRV.

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:

Cystatin-C Mouse Recombinant, sf9

Cystatin-C, Cystatin-3, Cst3.

Product # :

PRO-2249

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Citations

Description

CST3 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 126 amino acids (21-140a.a.) and having a molecular mass of 14.2kDa. (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).CST3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

CST3 protein solution (1mg/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
Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.
Synonyms
Cystatin-C, Cystatin-3, Cst3.
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
ATPKQGPRML GAPEEADANE EGVRRALDFA VSEYNKGSND AYHSRAIQVV RARKQLVAGV NYFLDVEMGR TTCTKSQTNL TDCPFHDQPH LMRKALCSFQ IYSVPWKGTH SLTKFSCKNA 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:

Cystatin C Rat Recombinant

Cystatin-C, Cystatin-3, CYSC, MGC105556.

Product # :

PRO-438

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Shipping Method :

Shipped at Room temp

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Citations

Description

Total 134 AA, Mw: 14.93 kDa (calculated). N-terminal His-tag (14AA).

Source

Escherichia Coli.

Formulation

Filtered (0.4 micron) and lyophilized from 0.5 mg/ml in 0.03M Acetate buffer, pH 4.

Purity

Greater than 96% as determined by SDS-PAGE.

More Info

Introduction
Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.
Synonyms
Cystatin-C, Cystatin-3, CYSC, MGC105556.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
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; it does not show any change after two weeks at 4°C.
Solubility
Add 0.2 ml of 0.1M Acetate buffer pH4 and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 0.1mg/ml. In higher concentrations the solubility of this antigen is limited.
Amino Acid Sequence
MRGSHHHHHH GMASGTSRPP PRLLGAPQEA DASEEGVQRA LDFAVSEYNK GSNDAYHSRA IQVVRARKQLVAGINYYLDV EMGRTTCTKS QTNLTNCPFH DQPHLMRKAL CSFQIYSVPW KGTHTLTKSS.

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:

Cystatin 7 Human Recombinant

Cystatin-F, Cystatin-7, Cystatin-like metastasis-associated protein, CMAP, Leukocystatin, Cystatin 7, CST7, CMAP.

Product # :

PRO-2222

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Description

CST7 Human Recombinant produced in E. coli is a single polypeptide chain containing 132 amino acids (20-145) and having a molecular mass of 15.3kDa.CST7 is fused to a 7 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CST7 solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Cystatin 7 (CST7) is a glycosylated cysteine protease inhibitor with a putative role in immune regulation through inhibition of a unique target in the hematopoietic system. Cystatin-7 is comprised of multiple cystatin-like sequences. The superfamily is comprised of 3 inhibitory families: the type 1 cystatins (stefins), type 2 cystatins and the kininogens. Some members are active cysteine protease inhibitors, while others have lost or possibly never had this inhibitory activity. Type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in various human fluids and secretions. CST7 protein expression has been observed in numerous human cancer cell lines established from malignant tumors.
Synonyms
Cystatin-F, Cystatin-7, Cystatin-like metastasis-associated protein, CMAP, Leukocystatin, Cystatin 7, CST7, CMAP.
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
GPSPDTCSQD LNSRVKPGFP KTIKTNDPGV LQAARYSVEK FNNCTNDMFL FKESRITRAL VQIVKGLKYM LEVEIGRTTC KKNQHLRLDD CDFQTNHTLK QTLSCYSEVW VVPWLQHFEV PVLRCHHHHH HH.

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:

Alpha-2-HS-Glycoprotein Mouse Recombinant

Alpha-2-HS-glycoprotein, Countertrypin, Fetuin-A.

Product # :

PRO-2220

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Shipped with Ice Packs

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Description

AHSG produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 333 amino acids (19-345.a.) and having a molecular mass of 36.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). AHSG is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

AHSG protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
AHSG (fetuin-A) which is a glycoprotein present in the serum, is synthesized by hepatocytes. AHSG is one of the fetuin class of plasma binding proteins. It is involved in a number of functions, such as endocytosis, brain development and the formation of bone tissue. It is usually present in the cortical plate of the immature cerebral cortex and bone marrow hemopoietic matrix, hence it has been postulated that it participates in the development of the tissues. Yet, its exact significance is still vague. AHSG promotes endocytosis, hold opsonic properties and influences the mineral phase of the bone. Affinity for calcium and barium ions has been shown.
Synonyms
Alpha-2-HS-glycoprotein, Countertrypin, Fetuin-A.
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
APQGTGLGFR ELACDDPEAE QVALLAVDYL NNHLLQGFKQ VLNQIDKVKV WSRRPFGVVY EMEVDTLETT CHALDPTPLA NCSVRQLTEH AVEGDCDFHI LKQDGQFRVM HTQCHSTPDS AEDVRKLCPR CPLLTPFNDT NVVHTVNTAL AAFNTQNNGT YFKLVEISRA QNVPLPVSTL VEFVIAATDC TAKEVTDPAK CNLLAEKQHG FCKANLMHNL GGEEVSVACK LFQTQPQPAN ANAVGPVPTA NAALPADPPA SVVVGPVVVP RGLSDHRTYH DLRHAFSPVA SVESASGETL HSPKVGQPGA AGPVSPMCPG RIRHFKIHHH HHH.

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:

AITR Human Recombinant

TNFRSF18, AITR, CD357, GITR, GITR-D, Tumor necrosis factor receptor superfamily member 18, Activation-inducible TNFR family receptor, Glucocorticoid-induced TNFR-related protein, CD357, UNQ319/PRO364.

Product # :

CYT-925

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Citations

Description

AITR Human Recombinant produced in Sf9 Baculovirus is a single, glycosylated polypeptide chain containing 145 amino acids (26-162a.a.) and having a molecular mass of 15.6kDa (Migrates at 18-28kDa on SDS-PAGE under reducing conditions).AITR is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

sds-page

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Synonyms
TNFRSF18, AITR, CD357, GITR, GITR-D, Tumor necrosis factor receptor superfamily member 18, Activation-inducible TNFR family receptor, Glucocorticoid-induced TNFR-related protein, CD357, UNQ319/PRO364.
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
QRPTGGPGCG PGRLLLGTGT DARCCRVHTT RCCRDYPGEE CCSEWDCMCV QPEFHCGDPC CTTCRHHPCP PGQGVQSQGK FSFGFQCIDC ASGTFSGGHE GHCKPWTDCT QFGFLTVFPG NKTHNAVCVP GSPPAEPLEH HHHHH.
Background
AITR Human Recombinant: Unveiling its Role in Immune Regulation and Therapeutic Potential
1. Abstract
This research paper aims to provide a comprehensive exploration of the AITR Human Recombinant, a crucial receptor involved in immune regulation. By examining its structure, signaling pathways, biological functions, and implications in disease, we unravel the potential therapeutic applications of AITR in immune-related disorders.
2. Introduction
AITR, also known as TNFRSF18, is a receptor protein that plays a vital role in immune regulation. With its involvement in T-cell responses and immune tolerance, AITR has emerged as an intriguing target for therapeutic interventions in various immune-mediated conditions.
3. Structure and Signaling of AITR
AITR is a transmembrane receptor protein belonging to the tumor necrosis factor receptor superfamily. Its extracellular domain interacts with its ligand, glucocorticoid-induced TNFR-related protein (GITR) ligand, leading to downstream signaling events that modulate immune cell function.
4. Biological Functions of AITR
AITR activation influences T-cell responses by regulating T-cell activation, proliferation, and cytokine production. Additionally, AITR signaling can modulate the balance between effector and regulatory T-cell populations, thereby playing a role in immune tolerance and immune homeostasis.
5. AITR in Disease Pathology
AITR dysregulation has been associated with various immune-related disorders, including autoimmune diseases, cancer, and transplant rejection. Understanding the role of AITR in these pathologies may provide insights into potential therapeutic strategies targeting AITR signaling.
6. Therapeutic Potential of AITR
The unique role of AITR in immune regulation makes it an appealing target for therapeutic interventions. Modulation of AITR signaling holds promise for manipulating immune responses in the context of autoimmune diseases, cancer immunotherapy, and transplantation.
7. Conclusion and Future Perspectives
While our understanding of AITR and its functions has advanced significantly, further research is warranted to unravel its complex signaling pathways and therapeutic potential. Continued investigations into AITR biology will enhance our ability to develop targeted therapies for immune-related disorders.
What is the molecular weight/Mw of AITR Protein?
AITR Protein has a total Mw of 15.6kDa.

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

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

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

What is the amino acid sequence of AITR Protein?
QRPTGGPGCG PGRLLLGTGT DARCCRVHTT RCCRDYPGEE CCSEWDCMCV QPEFHCGDPC CTTCRHHPCP PGQGVQSQGK FSFGFQCIDC ASGTFSGGHE GHCKPWTDCT QFGFLTVFPG NKTHNAVCVP GSPPAEPLEH HHHHH.

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

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

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

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