Search: 1000 results found for "calreticulin"

Description:

Growth differentiation factor 10 Human Recombinant

Bone morphogenetic protein 3b, BMP-3b, Growth/differentiation factor 10, GDF-10, Bone-inducing protein, BIP, GDF10, BMP3B.

Product # :

CYT-659

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Description

GDF10 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids (369-478 a.a.) and having a total molecular mass of 12.5 kDa. GDF10 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GDF10 solution (1mg/ml) contains 10mM Sodium citrate (pH 3.5), 1mM DTT, 40% glycerol and 0.1M NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GDF10 is a member of the BMP family and the TGF-beta superfamily. GDF10 is expressed in femur, brain, lung, skeletal, muscle, pancreas and testis, and has a role in head formation and possibly multiple roles in skeletal morphogenesis. In humans, GDF10 mRNA is found in the cochlea and lung of fetuses, and in testis, retina, pineal gland, and other neural tissues of adults. The BMP family members are regulators of cell growth and differentiation in both embryonic and adult tissues. These proteins are characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing 7 conserved cysteine residues.
Synonyms
Bone morphogenetic protein 3b, BMP-3b, Growth/differentiation factor 10, GDF-10, Bone-inducing protein, BIP, GDF10, BMP3B.
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
MQWDEPRVCS RRYLKVDFAD IGWNEWIISP KSFDAYYCAG ACEFPMPKIV RPSNHATIQS IVRAVGIIPG IPEPCCVPDK MNSLGVLFLD ENRNVVLKVY PNMSVDTCAC R.
Background
What is the molecular weight/Mw of GDF10 HUMAN Protein?
GDF10 HUMAN Protein has a total Mw of 12.5kDa.

What is the source or expression system of GDF10 HUMAN Protein?
Escherichia Coli.

What is the Purity of GDF10 HUMAN Protein?
GDF10 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF10 HUMAN Protein?
The biological functionality of GDF10 HUMAN Protein will be determined in the future.

What is the amino acid sequence of GDF10 HUMAN Protein?
MQWDEPRVCS RRYLKVDFAD IGWNEWIISP KSFDAYYCAG ACEFPMPKIV RPSNHATIQS IVRAVGIIPG IPEPCCVPDK MNSLGVLFLD ENRNVVLKVY PNMSVDTCAC R.

What applications can GDF10 HUMAN Protein be used in?
GDF10 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF10 HUMAN Protein?
The endotoxin level is minimal, GDF10 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:

Leptin Antagonist Triple Mutant Rat Recombinant

Product # :

CYT-355

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Description

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

Source

Escherichia coli.

Formulation

The protein was lyophilized from a concentrated (0.85mg/ml) solution with 0.003mM NaHCO3.

Purity

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

Biological Activity

ProSpec’s Leptin Antagonist Triple Mutant Rat Recombinant 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 Rat Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP-tA 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 Rat Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with 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 quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.21 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:

LIN7C Human Recombinant

LIN-7-C, LIN-7C, MALS-3, MALS3, VELI3, Lin-7 homolog C, Protein lin-7 homolog C, Mammalian lin-seven protein 3, MALS-3, Veli-3, LIN7C, Vertebrate lin-7 homolog 3.

Product # :

PRO-1305

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Description

LIN7C Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-197 a.a.) and having a molecular mass of 24.2 kDa. LIN7C is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

LIN7C protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 30% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE

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Introduction
LIN7C has a part in establishing and preserving the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. LIN7C forms membrane-associated multiprotein complexes which regulate distribution and recycling of proteins to the appropriate membrane domains.
Synonyms
LIN-7-C, LIN-7C, MALS-3, MALS3, VELI3, Lin-7 homolog C, Protein lin-7 homolog C, Mammalian lin-seven protein 3, MALS-3, Veli-3, LIN7C, Vertebrate lin-7 homolog 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
MGCSHHHHHH SSGLVPRGSH MGSMAALGEP VRLERDICRA IELLEKLQRS GEVPPQKLQA LQRVLQSEFC NAVREVYEHV YETVDISSSP EVRANATAKA TVAAFAASEG HSHPRVVELP KTEEGLGFNI MGGKEQNSPI YISRIIPGGI ADRHGGLKRG DQLLSVNGVS VEGEHHEKAV ELLKAAQGKV KLVVRYTPKV LEEMESRFEK MRSAKRRQQT.

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:

Natriuretic Peptide A Human Recombinant

Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.

Product # :

CYT-1028

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Description

NPPA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 26-123) containing 106 amino acids including an 8 a.a N-terminal His tag. The total molecular mass is 11.7kDa (calculated).

Source

Escherichia Coli.

Formulation

NPPA filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer, 50 mM NaCl and 5% w/v trehalosa, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Natriuretic Peptide A (NPPA) is a part of the natriuretic peptide family and is involved in cardiovascular homeostasis through regulation of natriuresis, diuresis, and vasodilation. NPPA is synthesized as a great precursor which releases a peptide from the N-terminus with similarity to vasoactive peptide, cardiodilatin, and another peptide from the C-terminus with natriuretic-diuretic activity. In female pregnancy, NPPA is promoting trophoblast invasion and spiral artery remodeling in uterus.
Synonyms
Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.
Physical Appearance
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
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. NPPA is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHNP MYNAVSNADL MDFKNLLDHL EEKMPLEDEV VPPQVLSEPN EEAGAALSPL PEVPPWTGEV SPAQRDGGAL GRGPWDSSDR SALLKSKLRA LLTAPR.

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:

Ciliary-Neurotrophic Factor Mouse Recombinant

HCNTF, CNTF, Ciliary Neurotrophic Factor.

Product # :

CYT-139

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Description

Ciliary Neurotrophic Factor Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids and having a molecular mass of 22.6kDa. The CNTF 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:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Fully biologically active when compared to standard. The ED50 as determined by the dose-dependant stimulation of TF-1 cells is less than 35ng/ml, corresponding to a Specific Activity of 3.0×10⁴ IU/mg.

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Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.
Synonyms
HCNTF, CNTF, Ciliary Neurotrophic Factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Ciliary Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CNTF 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 CNTF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAFAEQSPLT LHRRDLCSRS IWLARKIRSD LTALMESYVK HQGLNKNISL DSVDGVPVAS TDRWSEMTEA ERLQENLQAY RTFQGMLTKL LEDQRVHFTP TEGDFHQAIH TLTLQVSAFA YQLEELMALL EQKVPEKEAD GMPVTIGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRVIS SHHMGISAHE SHYGAKQM
Background
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 22.6kDa.

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

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

What is the Biological Activity of CNTF Protein?
Fully biologically active when compared to standard. The ED50 as determined by the dose-dependant stimulation of TF-1 cells is less than 35ng/ml, corresponding to a Specific Activity of 3.0×104 IU/mg.

What is the amino acid sequence of CNTF Protein?
MAFAEQSPLT LHRRDLCSRS IWLARKIRSD LTALMESYVK HQGLNKNISL DSVDGVPVAS TDRWSEMTEA ERLQENLQAY RTFQGMLTKL LEDQRVHFTP TEGDFHQAIH TLTLQVSAFA YQLEELMALL EQKVPEKEAD GMPVTIGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRVIS SHHMGISAHE SHYGAKQM

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

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

MIG (CXCL9) Bovine Recombinant

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

Product # :

CHM-041

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Description

MIG (CXCL9) BovineRecombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 104 amino acids and having a molecular mass of approximately 18.0kDa.MIG is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in 20 mM PB and 500mM NaCl, pH 7.0.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity determined by a chemotaxis bioassay using human lymphocytes is 0.1-1.0 ng/ml.

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

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

What is the Purity of CXCL9 BOVINE Protein?
CXCL9 BOVINE Protein is > 96% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL9 BOVINE Protein?
The biological activity determined by a chemotaxis bioassay using human lymphocytes is 0.1-1.0 ng/ml.

What is the amino acid sequence of CXCL9 BOVINE Protein?
VPAIRNGRCS CINTSQGMIH PKSLKDLKQF APSPSCEKTE IIATMKNGNE ACLNPDLPEV KELIKEWEKQ VNQKKKQRKG KKYKKTKKVP KVKRSQRPSQ KKTT.

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

What is the endotoxin level for CXCL9 BOVINE Protein?
The endotoxin level is minimal, CXCL9 BOVINE 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:

Neurofilament Light Bovine

Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.

Product # :

PRO-2786

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Description

NEFL Bovine having a calculated molecular mass of 68 kDa, pI-5.0.

Source

Bovine spinal cord.

Formulation

NEFL was lyophilized from a 1mg/ml solution containing 10mM sodium phosphate buffer pH 7.5, 6M urea, 1mM EDTA, 2mM DTT and 10mM methylammonium chloride.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Synonyms
Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store the lyophilized NEFL between 2-8°C, do not freeze. Upon reconstitution NEFL should be stored at -20°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized NEFL in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Neurofilament light chain (NEFL) is a critical component of the neuronal cytoskeleton, primarily found in neurons of the central and peripheral nervous systems. While extensive research has been conducted on NEFL in human and rodent models, the study of NEFL in bovine nervous tissues is an emerging area with potential for advancing our understanding of neuronal biology in larger mammals and its applications in veterinary medicine and neurobiology.
Bovine nervous tissues, such as the brain and spinal cord, are of particular interest due to their relevance in cattle health and the food industry. This research aims to provide a comprehensive exploration of NEFL in bovine nervous tissues, elucidating its functions, structural significance, and potential applications.
The primary objective of this research is to elucidate the role of NEFL in bovine nervous tissues, particularly in maintaining the structural integrity of neurons and axons. In vitro and ex vivo experiments, utilizing bovine neuronal cell cultures and tissue specimens, will be conducted to investigate how NEFL contributes to neuronal morphology, axonal transport, and neuronal resilience. Understanding these mechanisms is fundamental for deciphering the complexities of neuronal biology in bovine species.
The second objective is to assess the relevance of bovine NEFL in veterinary medicine. Studies involving bovine models will be conducted to evaluate the impact of NEFL mutations or variations on neuronal health, disease susceptibility, and neurodegenerative conditions. These investigations may provide valuable insights into potential applications in cattle health and the development of diagnostic tools for neurological disorders.
The third objective is to explore the potential applications of bovine NEFL in neurobiology and biotechnology. Research will investigate the use of bovine NEFL-expressing cells as models for studying neuronal-related diseases and for developing tissue engineering approaches for veterinary medicine and biotechnology.
By delving into the functions and roles of NEFL in bovine nervous tissues, this research aims to expand our knowledge of neuronal biology, its implications for veterinary medicine, and its potential applications in neurobiology and cattle health

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:

Septin-2 Human Recombinant

Septin 2, DIFF6, NEDD5, hNedd5, Pnutl3, NEDD-5.

Product # :

PRO-255

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Description

SEPT2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 381 amino acids (1-361 a.a.) and having a molecular mass of 43.6kDa. SEPT2 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SEPT2 solution (0.25mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
SEPT2 is a GTPase which is mandatory for cytokinesis and related to exocytosis. Septin-2 protein is able to hetero-oligomerize with Septin6, 7 and in addition takes part in the organization of new growth in organisms. SEPT2 is associated with a Tau-based paired helical filament core and contributes to the creation of neurofibrillary tangle as integral constituents of paired helical filaments.
Synonyms
Septin 2, DIFF6, NEDD5, hNedd5, Pnutl3, NEDD-5.
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 MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK STLINSLFLT DLYPERVISG AAEKIERTVQ IEASTVEIEE RGVKLRLTVV DTPGYGDAIN CRDCFKTIIS YIDEQFERYL HDESGLNRRH IIDNRVHCCF YFISPFGHGL KPLDVAFMKA IHNKVNIVPV IAKADTLTLK ERERLKKRIL DEIEEHNIKI YHLPDAESDE DEDFKEQTRL LKASIPFSVV GSNQLIEAKG KKVRGRLYPW GVVEVENPEH NDFLKLRTML ITHMQDLQEV TQDLHYENFR SERLKRGGRK VENEDMNKDQ ILLEKEAELR RMQEMIARMQ AQMQMQMQGG DGDGGALGHH V.

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:

Troponin I Skeletal Muscle Human

DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle, Troponin I, slow-twitch isoform.

Product # :

PRO-2789

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Description

TNNI1 Native produced in Human skeletal is Immunological identity confirmed by reaction with monoclonal antibody that is specific for the Human Troponin I Skeletal Muscle. TNNI1 Native is purified by proprietary chromatographic technique.

Source

Human skeletal muscle.

Formulation

TNNI1 was lyophilized from 0.01M HCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Synonyms
DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle, Troponin I, slow-twitch isoform.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Troponin I Skeletal Muscle although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNI1 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 TNNI1 in Tris/urea buffer (20mM Tris, pH 7.5, 7M urea, 5mM EDTA, 15mM 2-mercaptoethanol) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Troponin I, specifically the skeletal muscle isoform encoded by the TNNI1 gene, is a crucial regulator of muscle contraction. It functions as part of the troponin complex, which controls the interaction between actin and myosin filaments during muscle contraction. While extensive research has been conducted on troponin I in the context of cardiac muscle and cardiac diseases, the study of native human skeletal muscle troponin I remains an important but relatively understudied area. This research aims to provide a comprehensive exploration of native human skeletal muscle troponin I (TNNI1), elucidating its functions, structural significance, and potential applications in musculoskeletal research and clinical medicine.
The primary objective of this research is to elucidate the physiological role of native human skeletal muscle TNNI1 in muscle contraction. Experiments involving human skeletal muscle tissue samples and isolated muscle fibers will be conducted to investigate how TNNI1 interacts with other components of the troponin complex and influences calcium-mediated muscle contraction. Understanding these mechanisms is fundamental for deciphering the complexities of skeletal muscle physiology and its implications for musculoskeletal health.
The second objective is to assess the clinical relevance of native TNNI1 in muscle-related diseases. Clinical studies involving patients with various neuromuscular and muscle-wasting conditions will be conducted to evaluate the diagnostic and prognostic value of TNNI1 as a biomarker. These investigations may provide valuable insights into the use of native TNNI1 in the early detection and management of muscle disorders.
The third objective is to explore the potential applications of native TNNI1 in musculoskeletal research and therapeutic development. Research will investigate the use of native TNNI1-expressing cells and tissues as models for studying muscle disorders and for developing novel therapeutic interventions targeting the troponin complex.
By delving into the functions and roles of native human skeletal muscle TNNI1, this research aims to expand our knowledge of skeletal muscle physiology, its implications for muscle-related diseases, and its potential applications in musculoskeletal research and clinical medicine.

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:

Maltose Binding Protein E.coli Recombinant, His Tag

Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

Product # :

PRO-2322

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Description

Recombinant E.Coli MBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (27-392 a.a) and having a molecular mass of 44.9kDa. MBP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MBP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.
Synonyms
Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.
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 MGSMKIEEGK LVIWINGDKG YNGLAEVGKK FEKDTGIKVT VEHPDKLEEK FPQVAATGDG PDIIFWAHDR FGGYAQSGLL AEITPDKAFQ DKLYPFTWDA VRYNGKLIAY PIAVEALSLI YNKDLLPNPP KTWEEIPALD KELKAKGKSA LMFNLQEPYF TWPLIAADGG YAFKYENGKY DIKDVGVDNA GAKAGLTFLV DLIKNKHMNA DTDYSIAEAA FNKGETAMTI NGPWAWSNID TSKVNYGVTV LPTFKGQPSK PFVGVLSAGI NAASPNKELA KEFLENYLLT DEGLEAVNKD KPLGAVALKS YEEELAKDPR IAATMENAQK GEIMPNIPQM SAFWYAVRTA VINAASGRQT VDEALKDAQT NSSSNNNNNN NNNNLGIEGR.

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:

Hematopoietic Cell Signal Transducer Human Recombinant

Hematopoietic Cell Signal Transducer, DNAX-Activation Protein 10, Phosphoinositide-3-Kinase Adaptor Protein, Transmembrane Adapter Protein KAP10, Kinase Assoc Pro Of ~10kDa, Membrane Protein DAP10, PIK3AP, DAP10, KAP10, Kinase Assoc Protein.

Product # :

PRO-2522

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Description

HCST produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 271 amino acids (20-48 a.a.) and having a molecular mass of 30.1kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).HCST is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

HCST protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
HCST (Hematopoietic Cell Signal Transducer) is part of the DAP10 family. HCST is capable of being a part of an immunoreceptor complex. HCST takes a vital part in inducing cytotoxicity against MHC class I chain-associated MICA & target cells expressing cell surface ligands such as UL16-binding protein (ULBP) & MICB. HCST complex participates in proliferation as well as cell survival by activating T & NK cell responses.
Synonyms
Hematopoietic Cell Signal Transducer, DNAX-Activation Protein 10, Phosphoinositide-3-Kinase Adaptor Protein, Transmembrane Adapter Protein KAP10, Kinase Assoc Pro Of ~10kDa, Membrane Protein DAP10, PIK3AP, DAP10, KAP10, Kinase Assoc Protein.
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
ADPTTPGERS SLPAFYPGTS GSCSGCGSLS LPLEPKSCDK 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:

Myostatin Human Recombinant

GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

Product # :

CYT-418

Price :

Quantity :

Shipping Method :

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Description

Myostatin Human Recombinant produced in E.Coli is a homodimer, non-glycosylated polypeptide chain containing 2 x 109 amino acids and having a total molecular mass of 24814 Dalton. The GDF-8 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 ED50 as determined by the inhibition of the proliferation of MPC-11 cells is < 20ng/ml, corresponding to a Specific Activity of 50,000units/mg.

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Introduction
GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.
Synonyms
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Myostatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Myostatin 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 Myostatin in sterile 20mM HCl at 0.1 mg/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 Asp-Phe-Gly-Leu-Asp.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.55 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Myostatin as a Reference Standard.

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

Description:

Oncostatin-M Mouse Recombinant

Oncostatin-M, OSM, OncoM.

Product # :

CYT-168

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Quantity :

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Description

OSM Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids and having a molecular mass of 20.4kDa.The OSM is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

OSM protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, 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 as determined by the dose-dependent stimulation of the proliferation of NIH-3T3 mouse embryonic fibroblast cells is < 1 ng/ml, corresponding to a specific activity of > 1.0×10⁶ units/mg.

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Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
Synonyms
Oncostatin-M, OSM, OncoM.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Oncostatin M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin 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 Oncostatin M in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
NRGCSNSSSQ LLSQLQNQAN LTGNTESLLE PYIRLQNLNT PDLRAACTQH SVAFPSEDTL RQLSKPHFLS TVYTTLDRVL YQLDALRQKF LKTPAFPKLD SARHNILGIR NNVFCMARLL NHSLEIPEPT QTDSGASRST TTPDVFNTKI GSCGFLWGYH RFMGSVGRVF REWDDGSTRS R.

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:

LIN7A Human Recombinant

Protein lin-7 homolog A, Lin-7A, hLin-7, Mammalian lin-seven protein 1, MALS-1, Tax interaction protein 33, TIP-33, Vertebrate lin-7 homolog 1, Veli-1, LIN7A, MALS1, VELI1, LIN7.

Product # :

PRO-1252

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Quantity :

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Description

LIN7A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 256 amino acids (1-233 a.a.) and having a molecular mass of 28.4kDa.LIN7A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

LIN7A protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE

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Introduction
Lin7A is a member of the lin-7 family. Lin7A is comprised of one L27 domain and one PDZ (DHR) domain. Lin7A plays a part in launching and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Lin7A is expressed in the brain, testis, kidney, placenta and liver.
Synonyms
Protein lin-7 homolog A, Lin-7A, hLin-7, Mammalian lin-seven protein 1, MALS-1, Tax interaction protein 33, TIP-33, Vertebrate lin-7 homolog 1, Veli-1, LIN7A, MALS1, VELI1, LIN7.
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 MGSMLKPSVT SAPTADMATL TVVQPLTLDR DVARAIELLE KLQESGEVPV HKLQSLKKVL QSEFCTAIRE VYQYMHETIT VNGCPEFRAR ATAKATVAAF AASEGHSHPR VVELPKTDEG LGFNVMGGKE QNSPIYISRI IPGGVAERHG GLKRGDQLLS VNGVSVEGEH HEKAVELLKA AKDSVKLVVR YTPKVLEEME ARFEKLRTAR RRQQQQLLIQ QQQQQQQQQT QQNHMS.

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:

Neuropilin 1 Mouse Recombinant

Neuropilin-1, A5 protein, CD304, Nrp1, Nrp.

Product # :

CYT-971

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Description

NRP1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 843 amino acids (22-856 a.a.) and having a molecular mass of 94.7kDa (Migrates at 100-150kDa on SDS-PAGE under reducing conditions).NRP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

NRP1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Neuropilin 1 (Nrp1) is a transmembrane glycoprotein which functions as a co-receptor for several extracellular ligands including class III/IV semaphorins, some isoforms of vascular endothelial growth factor and transforming growth factor beta. Nrp1 binds vascular endothelial growth factor (VEGF)-A and is believed to serve as a coreceptor for kinase insert domain-containing receptor (KDR) by connecting with KDR and enhancing VEGF signaling. Nrp1 is a marker of regulatory T cells.
Synonyms
Neuropilin-1, A5 protein, CD304, Nrp1, Nrp.
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
FRSDKCGGTI KIENPGYLTS PGYPHSYHPS EKCEWLIQAP EPYQRIMINF NPHFDLEDRD CKYDYVEVID GENEGGRLWG KFCGKIAPSP VVSSGPFLFI KFVSDYETHG AGFSIRYEIF KRGPECSQNY TAPTGVIKSP GFPEKYPNSL ECTYIIFAPK MSEIILEFES FDLEQDSNPP GGMFCRYDRL EIWDGFPEVG PHIGRYCGQK TPGRIRSSSG VLSMVFYTDS AIAKEGFSAN YSVLQSSISE DFKCMEALGM ESGEIHSDQITASSQYGTNW SVERSRLNYP ENGWTPGEDS YKEWIQVDLG LLRFVTAVGT QGAISKETKK KYYVKTYRVD ISSNGEDWIS LKEGNKAIIF QGNTNPTDVV LGVFSKPLIT RFVRIKPVSW ETGISMRFEV YGCKITDYPC SGMLGMVSGL ISDSQITASN QADRNWMPEN IRLVTSRTGW ALPPSPHPYT NEWLQVDLGD EKIVRGVIIQ GGKHRENKVF MRKFKIAYSN NGSDWKTIMD DSKRKAKSFE GNNNYDTPEL RTFSPLSTRF IRIYPERATH SGLGLRMELL GCEVEAPTAG PTTPNGNPVD ECDDDQANCH SGTGDDFQLT GGTTVLATEK PTIIDSTIQS EFPTYGFNCE FGWGSHKTFC HWEHDSHAQL RWSVLTSKTG PIQDHTGDGN FIYSQADENQ KGKVARLVSP VVYSQSSAHC MTFWYHMSGS HVGTLRVKLR YQKPEEYDQL VWMVVGHQGD HWKEGRVLLH KSLKLYQVIF EGEIGKGNLG GIAVDDISIN NHISQEDCAK PTDLDKKNTE IKIDETGSTP GYEGEGEGDK NISRKPGNVL KTLDPLEHHH 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:

Leptin Dog Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-506

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

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

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

Purity

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

Biological Activity

Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

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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.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.20 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:

Stanniocalcin-2 Human Recombinant

Stanniocalcin-2, STC, STC2, STCRP, STC-2, Stanniocalcin-related protein, STC-related protein.

Product # :

HOR-296

Price :

Quantity :

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source
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Description

Stanniocalcin-2 Human Recombinant produced in HEK 293 cell line is a single, glycosylated, polypeptide chain containing 289 amino acids and having a total molecular mass of 31.9kDa (calculated). The Stanniocalcin contains four extra residues which were used as a spacer and 8 residues form the C-Terminal Flag- tag.Stanniocalcin is purified by proprietary chromatographic techniques.The amino acid sequence of the recombinant human Stanniocalcin-2 is 100% homologous to the amino acid sequence AA 25-302 of the human mature Human Stanniocalcin-2.

Source

HEK 293 cell line (Human embryonic kidney).

Formulation

Filtered (0.4µm) and lyophilized in 0.5mg/ml in 20mM Tris buffer, 20mM NaCl, pH 7.5.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
STC2 is a homodimeric glycoprotein that is expressed in a wide variety of tissues and may have autocrine or paracrine functions. The encoded protein has 10 of its 15 cysteine residues conserved among stanniocalcin family members and is phosphorylated by casein kinase 2 exclusively on its serine residues. Its C-terminus contains a cluster of histidine residues which may interact with metal ions. The protein may play a role in the regulation of renal and intestinal calcium and phosphate transport, cell metabolism, or cellular calcium/phosphate homeostasis. Constitutive over expression of human stanniocalcin 2 in mice resulted in pre- and postnatal growth restriction, reduced bone and skeletal muscle growth, and organomegaly. Expression of this gene is induced by estrogen and altered in some breast cancers.
Synonyms
Stanniocalcin-2, STC, STC2, STCRP, STC-2, Stanniocalcin-related protein, STC-related protein.
Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized STC-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Stanniocalcin 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
Add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
TDATNPPEGP QDRSSQQKGR LSLQNTAEIQ HCLVNAGDVG CGVFECFENN SCEIRGLHGI CMTFLHNAGKFDAQGKSFIK DALKCKAHAL RHRFGCISRK CPAIREMVSQ LQRECYLKHD LCAAAQENTR VIVEMIHFKDLLLHEPYVDL VNLLLTCGEE VKEAITHSVQ VQCEQNWGSL CSILSFCTSA IQKPPTAPPE RQPQVDRTKLSRAHHGEAGH HLPEPSSRET GRGAKGERGS KSHPNAHARG RVGGLGAQGP SGSSEWEDEQ SEYSDIRRAAADYKDDDDK.

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:

Cytotoxic T-Lymphocyte Associated Antigen-4 Human Recombinant, igG-His Tag

CTLA4, ALPS5, CD, CD152, CELIAC3, CTLA-4, GRD4, GSE, IDDM12, CD152, Cytotoxic T-Lymphocyte Associated Antigen-4, igG-His Tag.

Product # :

CYT-985

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Description

CTLA4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 368 amino acids (36-161a.a.) and having a molecular mass of 40.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CTLA4 is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

CTLA4 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
CTLA-4 is a member of the immunoglobulin superfamily and encodes a protein which transmits an inhibitory signal to T cells. The protein contains a V domain, a transmembrane domain, and a cytoplasmic tail. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. The membrane-bound isoform functions as a homodimer interconnected by a disulfide bond, while the soluble isoform functions as a monomer. Mutations in this gene have been associated with insulin-dependent diabetes mellitus, Graves disease, Hashimoto thyroiditis, celiac disease, systemic lupus erythematosus, thyroid-associated orbitopathy, and other autoimmune diseases.
Synonyms
CTLA4, ALPS5, CD, CD152, CELIAC3, CTLA-4, GRD4, GSE, IDDM12, CD152, Cytotoxic T-Lymphocyte Associated Antigen-4, igG-His Tag.
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
ADLKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSDL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH.
Background
What is the molecular weight/Mw of CTLA4 Protein?
CTLA4 Protein has a total Mw of 40.8kDa.

What is the source or expression system of CTLA4 Protein?
Sf9, Baculovirus cells.

What is the Purity of CTLA4 Protein?
CTLA4 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CTLA4 Protein?
The biological functionality of CTLA4 Protein will be determined in the future.

What is the amino acid sequence of CTLA4 Protein?
ADLKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSDL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH.

What applications can CTLA4 Protein be used in?
CTLA4 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CTLA4 Protein?
The endotoxin level is minimal, CTLA4 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:

MIG Human Recombinant (CXCL9)

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

Product # :

CHM-333

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

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Introduction
Chemokine (C-X-C motif) ligand 9 (CXCL9) is a small cytokine belonging to the CXC chemokine family that is also known as Monokine induced by gamma INF (MIG). CXCL9 is a T-cell chemoattractant, which is induced by IFN-?. It is closely related to two other CXC chemokines called CXCL10 and CXCL11, whose genes are located near the gene for CXCL9 on human chromosome 4. CXCL9, CXCL10 and CXCL11 all elicit their chemotactic functions by interacting with the chemokine receptor CXCR3.
Synonyms
Small inducible cytokine B9, CXCL9, Gamma INF-induced monokine, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, monokine induced by gamma-INF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL9 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized MIG in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TPVVRKGRCSCISTNQGTIHLQSLKDLKQFAPSPSCEKIEIIATLKNGVQTCLNPDS
ADVKELIKKWEKQVSQKKKQKNGKKHQKKKVLKVRKSQRSRQKKTT.
Background
What is the molecular weight/Mw of CXCL9 HUMAN Protein?
CXCL9 HUMAN Protein has a total Mw of 11.7kDa.

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

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

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

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

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

What is the endotoxin level for CXCL9 HUMAN Protein?
The endotoxin level is minimal, CXCL9 HUMAN Protein was purified using conventional chromatography techniques.

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

Description:

Interleukin-33 Rat Recombinant, His Tag

Interleukin-33, IL-33.

Product # :

CYT-906

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Shipped with Ice Packs

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Description

IL 33 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids (109-264 a.a) and having a molecular mass of 19.8kDa. IL 33 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL 33 protein solution (0.5mg/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
nterleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.
Synonyms
Interleukin-33, IL-33.
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 MGSSIQGTSL LTESCALSTY NDQSVSFVLE NGCYVINVED CGKNQEKDKV LLRYYESSFP AQSGDGVDGK KLMVNMSPIK DTDIWLNAND KDYSVELQKG DVSPPDQAFF VLHKKSSDFV SFECKNLPGT YIGVKDNQLA LVEENDESCN NIMFKLSKM.

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:

CD33 Human Recombinant

CD33Molecule, CD33Antigen (Gp67), Sialic Acid Binding Ig-Like Lectin 3, Sialic Acid-Binding Ig-Like Lectin 3, SIGLEC3, gp67, SIGLEC-3, Myeloid Cell Surface AntigenCD33, p67, Siglec-3, CD33Antigen.

Product # :

PRO-1887

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Shipped with Ice Packs

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Description

CD33 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 265 amino acids (18-259 a.a) and having a molecular mass of 29.1kDa.CD33 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CD33 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea, and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
CD33 is putative adhesion molecule of myelomonocytic-derived cells which mediates sialic-acid dependent binding to cells. CD33 prefers to bind to alpha-2,6-linked sialic acid. The sialic acid recognition site is masked by cis interactions with sialic acids on the same cell surface. In the immune response, CD33 perform as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatases through their SH2 domains which block signal transduction through dephosphorylation of signaling molecules. In addition, CD33 induces apoptosis in acute myeloid leukemia.
Synonyms
CD33Molecule, CD33Antigen (Gp67), Sialic Acid Binding Ig-Like Lectin 3, Sialic Acid-Binding Ig-Like Lectin 3, SIGLEC3, gp67, SIGLEC-3, Myeloid Cell Surface AntigenCD33, p67, Siglec-3, CD33Antigen.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDPNFWLQ VQESVTVQEG LCVLVPCTFF HPIPYYDKNS PVHGYWFREG AIISGDSPVA TNKLDQEVQE ETQGRFRLLG DPSRNNCSLS IVDARRRDNG SYFFRMERGS TKYSYKSPQL SVHVTDLTHR PKILIPGTLE PGHSKNLTCS VSWACEQGTP PIFSWLSAAP TSLGPRTTHS SVLIITPRPQ DHGTNLTCQV KFAGAGVTTE RTIQLNVTYV PQNPTTGIFP GDGSGKQETR AGVVH.

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:

Desmin Chicken Gizzard

Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.

Product # :

PRO-2783

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Shipped at Room temp

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Description

Desmin Chicken having a calculated molecular mass of 53 kDa, pI-5.4.

Source

Chicken gizzard.

Formulation

Desmin was lyophilized from a 1mg/ml solution containing 10 mM sodium phosphate buffer pH 7.5, 6M urea, 1mM EDTA, 2mM DTT and 10mM methylammonium chloride.

Purity

Greater than 98.0% as determined by SDS-PAGE.

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Synonyms
Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Store the lyophilized Desmin between 2-8°C, do not freeze. Upon reconstitution Desmin should be stored at -20°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Desmin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Desmin, an intermediate filament protein, plays a fundamental role in maintaining the structural integrity and function of muscle cells. While extensive research has been conducted on desmin in mammals, the study of desmin in chickens is an emerging area with considerable potential for advancing our understanding of muscle biology. Chickens are valuable model organisms for studying muscle development, growth, and regeneration due to their relatively simple muscular system and economic significance in poultry production. This research aims to provide a comprehensive exploration of desmin in chickens, shedding light on its functions and implications for muscle structure and function.
The primary objective of this research is to elucidate the role of desmin in chicken muscle structure and development. In vitro and in vivo experiments, utilizing chicken cell cultures and embryonic models, will be conducted to investigate how desmin contributes to the organization of muscle fibers, sarcomere assembly, and myofibrillogenesis. Understanding these mechanisms is fundamental for deciphering the complexities of muscle development in chickens.
The second objective is to assess the clinical and economic relevance of desmin in poultry production. Studies involving broiler chickens will be conducted to evaluate the impact of desmin mutations or variations on muscle growth, meat quality, and disease susceptibility. These investigations may provide valuable insights into potential strategies for enhancing poultry production efficiency and meat quality.
The third objective is to explore the potential applications of desmin in biotechnology and tissue engineering. Research will investigate the use of desmin-expressing chicken cells as models for studying muscle-related diseases and for developing tissue engineering approaches for muscle repair and regeneration.
By delving into the functions and roles of desmin in chickens, this research aims to expand our knowledge of muscle biology, its implications for poultry production, and its potential applications in biotechnology and regenerative medicine.

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:

VEGF Co-regulated Chemokine 1, His Tag Human Recombinant

Dcip1, DMC, MGC138300, UNQ473, VCC-1, VCC1, VEGF coregulated chemokine 1, C-X-C motif chemokine 17, Dendritic cell and monocyte chemokine-like protein.

Product # :

CHM-024

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Shipping Method :

Shipped with Ice Packs

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SDS-PAGE

Description

CXCL17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids (22-119 a.a) and having a molecular mass of 13.7kDa.CXCL17 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CXCL17 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Dendritic cell and monocyte chemokinelike protein (DMC/CXCL17/VEGF-correlated chemokine 1/VCC1), is a secreted molecule with a size and predicted 3-dimensional folding pattern similar to that of chemokines CXCL8/IL8 and CXCL14/BRAK. CXCL17 is constitutively generated by airway and intestinal epithelium. CXCL17 induces the chemotaxis of quiescent, but not LPS-activated peripheral blood monocytes and dendritic cells, and it also binds these cells specifically. The expression of CXCL17 is increased in endothelial cells when they are induced to form tubes in vitro. CXCL17, CXCL1/GRO and CXCL8/IL8 which have roles in angiogenesis, show significantly correlated expression with that of VEGF in primary lung, breast and esophageal tumors. Therefore, CXCL17 is suggested to have a role in tumor angiogenesis. The mature Rat CXCL17 shares 82%, 71% amino acid sequence identity with mouse, human CXCL17, respectively.
Synonyms
Dcip1, DMC, MGC138300, UNQ473, VCC-1, VCC1, VEGF coregulated chemokine 1, C-X-C motif chemokine 17, Dendritic cell and monocyte chemokine-like 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
MGSSHHHHHH SSGLVPRGSH MSSLNPGVAR GHRDRGQASR RWLQEGGQEC ECKDWFLRAP RRKFMTVSGL PKKQCPCDHF KGNVKKTRHQ RHHRKPNKHS RACQQFLKQC QLRSFALPL.
Background
What is the molecular weight/Mw of CXCL17 HUMAN, HIS Protein?
CXCL17 HUMAN, HIS Protein has a total Mw of 13.7kDa.

What is the source or expression system of CXCL17 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of CXCL17 HUMAN, HIS Protein?
CXCL17 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL17 HUMAN, HIS Protein?
The biological functionality of CXCL17 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CXCL17 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MSSLNPGVAR GHRDRGQASR RWLQEGGQEC ECKDWFLRAP RRKFMTVSGL PKKQCPCDHF KGNVKKTRHQ RHHRKPNKHS RACQQFLKQC QLRSFALPL.

What applications can CXCL17 HUMAN, HIS Protein be used in?
CXCL17 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL17 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL17 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:

Sialic Acid Binding Ig Like Lectin 9 Human Recombinant

Sialic Acid Binding Ig Like Lectin 9, Protein FOAP-9, Siglec-9, CDw329, Sialic Acid Binding Ig-Like Lectin 9, Sialic Acid-Binding Ig-Like Lectin 9, CD329 Antigen, OBBP-LIKE, FOAP-9, CD329.

Product # :

PRO-2447

Price :

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Shipping Method :

Shipped with Ice Packs

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Description

SIGLEC9 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 573 amino acids (18-348a.a.) and having a molecular mass of 63.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).SIGLEC9 is expressed with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

SIGLEC9 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
Sialic Acid Binding Ig Like Lectin 9 (SIGLEC9) is a member of the sialic acid-binding Ig-like lectin family, which is a part of the immunoglobulin superfamily expressed mostly on human blood leukocytes. SIGLEC9 is a Putative adhesion molecule which is expressed in bone marrow, placenta, spleen, and fetal liver. SIGLEC9 is also a part of the recently characterized CD33-related Siglec family of sialic acid binding protein.
Synonyms
Sialic Acid Binding Ig Like Lectin 9, Protein FOAP-9, Siglec-9, CDw329, Sialic Acid Binding Ig-Like Lectin 9, Sialic Acid-Binding Ig-Like Lectin 9, CD329 Antigen, OBBP-LIKE, FOAP-9, CD329.
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
ADPQTSKLLT MQSSVTVQEG LCVHVPCSFS YPSHGWIYPG PVVHGYWFRE GANTDQDAPV ATNNPARAVW EETRDRFHLL GDPHTKNCTL SIRDARRSDA GRYFFRMEKG SIKWNYKHHR LSVNVTALTH RPNILIPGTL ESGCPQNLTC SVPWACEQGT PPMISWIGTS VSPLDPSTTR SSVLTLIPQP QDHGTSLTCQ VTFPGASVTT NKTVHLNVSY PPQNLTMTVF QGDGTVSTVL GNGSSLSLPE GQSLRLVCAV DAVDSNPPAR LSLSWRGLTL CPSQPSNPGV LELPWVHLRD AAEFTCRAQN PLGSQQVYLN VSLQSKATSG VTQGLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH 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.

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