Search results
1000 results found for “Tachykinin”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
CCNB2 HumanDescription:
Cyclin-B2 Human Recombinant
G2/mitotic-specific cyclin-B2, HsT17299, cyclin B2.
Product # :
PKA-035Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CCNB2 Human Recombinant produced in E. coli is a single polypeptide chain containing 422 amino acids (1-398) and having a molecular mass of 47.9 kDa.CCNB2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CCNB2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 5mM DTT and 50% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
CCNB2 is a member of the cyclin family. CCNB2 is vital for regulation of the cell cycle at the G2/M (mitosis) transition. CCNB2 cooperates with the CDK1 protein kinase to create a serine/threonine kinase holoenzyme complex recognized as maturation promoting factor (MPF).
-
Synonyms
G2/mitotic-specific cyclin-B2, HsT17299, cyclin B2.
-
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 MGSHMALLRR PTVSSDLENI DTGVNSKVKS HVTIRRTVLE EIGNRVTTRA AQVAKKAQNT KVPVQPTKTT NVNKQLKPTA SVKPVQMEKL APKGPSPTPE DVSMKEENLC QAFSDALLCK IEDIDNEDWE NPQLCSDYVK DIYQYLRQLE VLQSINPHFL DGRDINGRMR AILVDWLVQV HSKFRLLQET LYMCVGIMDR FLQVQPVSRK KLQLVGITAL LLASKYEEMF SPNIEDFVYI TDNAYTSSQI REMETLILKE LKFELGRPLP LHFLRRASKA GEVDVEQHTL AKYLMELTLI DYDMVHYHPS KVAAAASCLS QKVLGQGKWN LKQQYYTGYT ENEVLEVMQH MAKNVVKVNE NLTKFIAIKN KYASSKLLKI SMIPQLNSKA VKDLASPLIG RSc
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.
- View Data Sheet
Name :
TIMP1 Human, HEKDescription:
Tissue Inhibitor of Metalloprotease 1 Human Recombinant, HEK
Metalloproteinase inhibitor 1, Tissue inhibitor of metalloproteinases, TIMP-1, Erythroid-potentiating activity, EPA, TIMP1, CLGI, TIMP, EPO, HCI, FLJ90373.
Product # :
ENZ-508Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
TIMP1 Human Recombinant produced in HEK-293 cells is a secreted protein with the sequence of Human TIMP-1 (amino acids Cys24-Ala207) and fused to a polyhistidine tag at the C-terminus.
Source
HEK293 Cells.
Formulation
The TIMP1 protein was lyophilized after extensive dialysis against PBS.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The IC50 of 2.5-4 nM is measured by its ability to inhibit recombinant human MMP-2 cleavage of the colorimetric peptide substrate, Mca-PLGL-DpaAR-NH2.More Info
-
Introduction
TIMP1 is a member of the TIMP family. TIMP1 is an inducible glycoprotein produced by various cell types. The TIMP1 glycoprotein is a natural inhibitor of the matrix metalloproteinases, which a group of peptidases involved in degradation of the extracellular matrix. TIMP1 binds in a reversible mode to MMPs, with regions in the N-terminal domain binding to the MMP substrate-binding site. On top of its inhibitory function against most of the known MMPs, TIMP1 is able to promote cell proliferation in a broad range of cell types, and may also have an anti-apoptotic role. Furthermore, TIMP1 has erthyroid-potentiating activity via translocation to the nucleus and also inhibits apoptosis in B-cells. The TIMP1 gene is situated within intron 6 of the synapsin I gene and is transcribed in the opposite direction. TIMP1 activity is dependent on the existence of disulfide bonds. TIMP1 transcription is extremely inducible in reaction to many cytokines and hormones. Increased TIMP1 levels are connecte
-
Synonyms
Metalloproteinase inhibitor 1, Tissue inhibitor of metalloproteinases, TIMP-1, Erythroid-potentiating activity, EPA, TIMP1, CLGI, TIMP, EPO, HCI, FLJ90373.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized TIMP1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TIMP1 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 TIMP1 in sterile 18M-cm H2O 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.
- View Data Sheet
Name :
MAO B HumanDescription:
Monoamine Oxidase B Human Recombinant
Amine oxidase [flavin-containing] B, Monoamine oxidase type B, MAO-B, MAOB, MGC26382.
Product # :
ENZ-440Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
MAO-B Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 488 amino acids fragment (2-489) corresponding to the cytoplasmic domain fragment of the mature protein, having a total molecular mass of 59.84kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The MAO-B is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MAO-B protein is supplied in 20mM Tris-HCl, pH 8.0, 250mM NaCl, 1mM EDTA and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
MAO-B is a member of the flavin monoamine oxidase family. MAO-B (Monoamine oxidase B) is a flavin-containing mitochondrial enzyme that catalyzes the oxidative deamination of biogenic and xenobiotic monoamines. MAO-B controls the metabolic degradation of catecholamines and serotonin in neural and other target tissues. MAO-B is located in platelets and in DOPA-secreting neurons in the brain. MAOB and MAOA genes have an imperative function in DOPA degradation. Benzylamine and phenylethylamine are preferentially degraded by MAOB. The MAOB gene is linked to autistic traits, empathy and Asperger syndrome. Amplified levels of MAO B are identified in the brain of Alzheimer’s patients. High phenylethylamine levels in neonates as a result of low MAOB are consistent with phenylketonuria in newborns. Polymorphisms in MAO-B are connected to smoking behavior.
-
Synonyms
Amine oxidase [flavin-containing] B, Monoamine oxidase type B, MAO-B, MAOB, MGC26382.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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.
- View Data Sheet
Name :
BPC-157Description:
BPC-157 Pentadecapeptide
Product # :
HOR-029Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
BPC-157 Synthetic is a single, non-glycosylated polypeptide chain containing 15 amino acids, having a molecular mass of 1419.55 Dalton and a Molecular formula of C62H98N16O22.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized BPC-157 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution bpc-157 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 BPC-157 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
H-Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val-OH
-
Background
BPC-157, short for Body Protection Compound-157, is a synthetic peptide that has garnered significant attention in the field of regenerative medicine and sports science. This peptide, derived from a portion of the human gastric juice protein known as BPC, exhibits remarkable healing and tissue regeneration properties. BPC-157 has shown promise in various preclinical and clinical studies, demonstrating its potential for the treatment of a wide range of injuries and disorders.
The research on BPC-157 encompasses investigations into its mechanisms of action, efficacy, safety, and potential therapeutic applications. Studies have elucidated the peptide's ability to enhance angiogenesis, promote collagen synthesis, modulate inflammatory responses, and protect against oxidative stress. These properties make BPC-157 an intriguing candidate for accelerating tissue healing, reducing inflammation, and improving overall recovery outcomes.
Preclinical studies have revealed the beneficial effects of BPC-157 in several injury models. For instance, BPC-157 has demonstrated its potential in accelerating tendon and ligament healing, mitigating muscle damage, and promoting bone regeneration. These findings suggest that BPC-157 could be a valuable therapeutic tool in orthopedic medicine and sports-related injuries.
Furthermore, BPC-157 has exhibited promising effects on gastrointestinal health. Studies have highlighted its ability to protect and heal the gut lining, reduce ulcer formation, and alleviate symptoms associated with inflammatory bowel disease. These observations open up avenues for BPC-157 as a potential treatment for gastrointestinal disorders.
In addition to its regenerative properties, BPC-157 has shown potential in neurological and psychiatric conditions. Research has indicated its neuroprotective effects, with implications for the treatment of traumatic brain injury, stroke, and neurodegenerative disorders. Preliminary studies also suggest BPC-157's potential as an antidepressant and anxiolytic agent.
Despite the promising findings, further research is needed to fully understand the mechanisms underlying BPC-157's actions and to assess its long-term safety and efficacy. Clinical trials are underway to explore its potential therapeutic applications in humans, including its use in tendon and ligament repair, inflammatory bowel disease, and neurodegenerative disorders.
This comprehensive review aims to summarize the current state of research on BPC-157, providing an overview of its mechanisms of action and therapeutic potential. By examining relevant studies and findings, we aim to shed light on the diverse applications of BPC-157 and its implications for regenerative medicine, sports science, and various disease
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
p85a BovineDescription:
Phosphoinositide 3-kinase a, regulatory subunit Bovine Recombinant
Phosphatidylinositol 3-kinase regulatory subunit alpha, PI3-kinase p85 subunit alpha, PtdIns-3-kinase p85-alpha, PI3K, P85a.
Product # :
PKA-328Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Phosphoinositide 3-kinase subunit p85a Bovine Recombinant has a molecular weight of 83.5 kDa.
Source
Leishmania tarentolae.
Formulation
Supplied as a 1 mg/ml solution in 25mM HEPES, pH 8.0, 25mM NaCl, 2.5mM MgCl2 and 50% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
P85a functions as the regulatory subunit of the class IA PI3-kinase isoforms a, b, and d.
It contains two SH2 domains that bind to tyrosine-phosphorylated growth factor receptors or substrate adaptor proteins.
It also contains a BH (breakpoint cluster region homology) domain that shows GAP activity towards the small GTPases Rab4, Rab5, Cdc42, Rac1 and to a lesser extend towards Rab6 and Rab11.
It was shown that PI3Ka catalytic subunit mediated phosphorylation of the p85a adapter reduces the lipid kinase activity of the heterodimer and this gives hints for PI3K-dependent signaling events not requiring production of 3’-phosphorylated phosphoinositides.
PI3Ka protein kinase activity has been implicated in IRS-1 serine phosphorylation in insulin-treated adipocytes and in STAT3 and IRS-1 phosphorylation upon activation of the type 1 IFN receptor by IFN-a. -
Synonyms
Phosphatidylinositol 3-kinase regulatory subunit alpha, PI3-kinase p85 subunit alpha, PtdIns-3-kinase p85-alpha, PI3K, P85a.
-
Physical Appearance
Sterile filtered liquid formualtion.
-
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.
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.
- View Data Sheet
Name :
ACTN1 HumanDescription:
Actinin Alpha 1 Human Recombinant
ACTN1, Actinin, Alpha 1, Alpha-Actinin Cytoskeletal Isoform, F-Actin Cross-Linking Protein, Non-Muscle Alpha-Actinin-1, BDPLT15, Actinin 1 Smooth Muscle, Alpha-Actinin-1.
Product # :
PRO-2227Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ACTN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 274 amino acids (1-249 a.a) and having a molecular mass of 31.4kDa. ACTN1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ACTN1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
ACTN1 encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.
-
Synonyms
ACTN1, Actinin, Alpha 1, Alpha-Actinin Cytoskeletal Isoform, F-Actin Cross-Linking Protein, Non-Muscle Alpha-Actinin-1, BDPLT15, Actinin 1 Smooth Muscle, Alpha-Actinin-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
MGSSHHHHHH SSGLVPRGSH MGSEFMDHYD SQQTNDYMQP EEDWDRDLLL DPAWEKQQRK TFTAWCNSHL RKAGTQIENI EEDFRDGLKL MLLLEVISGE RLAKPERGKM RVHKISNVNK ALDFIASKGV KLVSIGAEEI VDGNVKMTLG MIWTIILRFA IQDISVEETS AKEGLLLWCQ RKTAPYKNVN IQNFHISWKD GLGFCALIHR HRPELIDYGK LRKDDPLTNL NTAFDVAEKY LDIPKMLDAE DIVGTARPDE KAIMTYVSSF YHAF.
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.
- View Data Sheet
Name :
CXCL17 RatDescription:
VEGF Co-regulated Chemokine 1 Rat Recombinant
Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.
Product # :
CHM-281Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CXCL17 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 97 amino acids and having a molecular mass of 11.5kDa.The CXCL17 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL17 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, 300mM NaCl, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED50 for this effect is typically 1-5 µg/ml.More Info
-
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
Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized CXCL17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL17 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 CXCL17 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.
-
Background
What is the molecular weight/Mw of CXCL17 RAT Protein?
CXCL17 RAT Protein has a total Mw of 11.5kDa.
What is the source or expression system of CXCL17 RAT Protein?
Escherichia Coli.
What is the Purity of CXCL17 RAT Protein?
CXCL17 RAT Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL17 RAT Protein?
Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED50 for this effect is typically 1-5 µg/ml.
What is the amino acid sequence of CXCL17 RAT Protein?
SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.
What applications can CXCL17 RAT Protein be used in?
CXCL17 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL17 RAT Protein?
The endotoxin level is minimal, CXCL17 RAT Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ANXA3 HumanDescription:
Annexin A3 Human Recombinant
ANX3, ANXA3, Annexin-III, Lipocortin-3, Lipocortin-III, Annexin-3, Annexin A3, Placental anticoagulant protein III, PAP-III, 35-alpha calcimedin, Inositol 1,2-cyclic phosphate 2-phosphohydrolase.
Product # :
PRO-765Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ANXA3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-323 a.a.) and having a molecular mass of 36.3 kDa. ANXA3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ANXA3 protein solution contains 20mM Tris-HCl, pH-7.5, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
ANXA3 is an inhibitor of phospholipase A2. ANXA3 possesses anti-coagulant properties. ANXA3 cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate. ANXA3 is part of the annexin family which are members of the calcium-dependent phospholipid-binding protein family that are involved in the regulation of cellular growth and in signal transduction pathways. ANXA3 takes part as an anti-coagulation factor.
-
Synonyms
ANX3, ANXA3, Annexin-III, Lipocortin-3, Lipocortin-III, Annexin-3, Annexin A3, Placental anticoagulant protein III, PAP-III, 35-alpha calcimedin, Inositol 1,2-cyclic phosphate 2-phosphohydrolase.
-
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
MASIWVGHRG TVRDYPDFSP SVDAEAIQKA IRGIGTDEKM LISILTERSN AQRQLIVKEY QAAYGKELKD DLKGDLSGHF EHLMVALVTP PAVFDAKQLK KSMKGAGTNE DALIEILTTR TSRQMKDISQ AYYTVYKKSL GDDISSETSG DFRKALLTLA DGRRDESLKV DEHLAKQDAQ ILYKAGENRW GTDEDKFTEI LCLRSFPQLK LTFDEYRNIS QKDIVDSIKG ELSGHFEDLL LAIVNCVRNT PAFLAERLHR ALKGIGTDEF TLNRIMVSRS EIDLLDIRTE FKKHYGYSLY SAIKSDTSGD YEITLLKICG GDD.
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.
- View Data Sheet
Name :
SSR2 HumanDescription:
Signal Sequence Receptor, Beta Human Recombinant
HSD25, TLAP, TRAP-BETA, TRAPB, Translocon-associated protein subunit beta, Signal sequence receptor subunit beta, SSR-beta.
Product # :
PRO-1380Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SSR2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 155 amino acids (18-149a.a) and having a molecular mass of 16.8kDa. SSR2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SSR2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
The signal sequence receptor (SSR) is a glycosylated endoplasmic reticulum membrane receptor related with protein translocation across the ER membrane. The SSR consists of 2 subunits, a 34-kD glycoprotein (alpha-SSR or SSR1) and a 22-kD glycoprotein (beta-SSR or SSR2). The human beta-signal sequence receptor gene (SSR2) maps to chromosome bands 1q21-q23. Diseases correlated with SSR2 include calcaneonavicular coalition, and osteosarcoma, and among its related super-pathways are Viral mRNA Translation and Generic Transcription Pathway.
-
Synonyms
HSD25, TLAP, TRAP-BETA, TRAPB, Translocon-associated protein subunit beta, Signal sequence receptor subunit beta, SSR-beta.
-
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 MGSEEGARLL ASKSLLNRYA VEGRDLTLQY NIYNVGSSAA LDVELSDDSF PPEDFGIVSG MLNVKWDRIA PASNVSHTVV LRPLKAGYFN FTSATITYLA QEDGPVVIGS TSAPGQGGIL AQREFDRRFS PHFLD.
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.
- View Data Sheet
Name :
CXCL8 Porcine (1-72)Description:
Interleukin-8 (1-72 a.a) Porcine Recombinant (CXCL8)
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP, Alveolar macrophage chemotactic factor I.
Product # :
CHM-340Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Interleukin-8 Porcine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 78 amino acids and having a molecular mass of 9.1kDa. The IL8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity was determined by a chemotaxis bioassay using human peripheral blood neutrophils is in a concentration range of 20-200 ng/ml.More Info
-
Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
-
Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP, Alveolar macrophage chemotactic factor I.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Interleukin 8 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
ARVSAELRCQ CINTHSTPFH PKFIKELRVI ESGPHCENSE IIVKLVNGKE VCLDPKEKWV QKVVQIFLKR TEKQQQQQ.
-
Background
What is the molecular weight/Mw of CXCL8 PORCINE (1-72) Protein?
CXCL8 PORCINE (1-72) Protein has a total Mw of 9.1kDa.
What is the source or expression system of CXCL8 PORCINE (1-72) Protein?
Escherichia Coli.
What is the Purity of CXCL8 PORCINE (1-72) Protein?
CXCL8 PORCINE (1-72) Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 PORCINE (1-72) Protein?
The biological activity was determined by a chemotaxis bioassay using human peripheral blood neutrophils is in a concentration range of 20-200 ng/ml.
What is the amino acid sequence of CXCL8 PORCINE (1-72) Protein?
ARVSAELRCQ CINTHSTPFH PKFIKELRVI ESGPHCENSE IIVKLVNGKE VCLDPKEKWV QKVVQIFLKR TEKQQQQQ.
What applications can CXCL8 PORCINE (1-72) Protein be used in?
CXCL8 PORCINE (1-72) Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 PORCINE (1-72) Protein?
The endotoxin level is minimal, CXCL8 PORCINE (1-72) 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.
- View Data Sheet
Name :
CALB1 HumanDescription:
Calbindin-1 Human Recombinant
Calbindin, Vitamin D-dependent calcium-binding protein, avian-type, Calbindin D28, D-28K, CALB1, CAB27, CALB, calbindin 1 28kDa.
Product # :
PRO-721Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CALB1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 261 amino acids (1-261 a.a.) and having a molecular mass of 30kDa.The CALB1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CALB1 protein solution contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 10% glycerol and 2mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Calbindin 1 (CALB1) is a calcium binding protein that is a member of the troponin C superfamily. CALB1 plays a vital role in calcium regulation (including calcium transport and uptake, calcification of bone and teeth) and calcium associated signaling in neurons and transiently in embryological development. CALB1 also has a role in protecting neurons from apoptotic cell death. CALB1 buffers cytosolic calcium and may stimulate a membrane Ca2+-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase. The biological function of CALB1 seems to be tied to the redox state of its five cysteine residues.
CALB1 has 4 active calcium-binding domains, and 2 modified domains that seemingly have lost their calcium-binding ability. CALB1 is expressed in neural tissues. In the brain, the CALB1 synthesis is independent of vitamin-D-derived hormones.
Disregulation of the CALB1 is associated with epilepsy, amyotrophic lateral sclerosis, Huntington's disease. The neurons in brains of Huntington disease patients are calbindin-depleted. -
Synonyms
Calbindin, Vitamin D-dependent calcium-binding protein, avian-type, Calbindin D28, D-28K, CALB1, CAB27, CALB, calbindin 1 28kDa.
-
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
MAESHLQSSL ITASQFFEIW LHFDADGSGY LEGKELQNLI QELQQARKKA GLELSPEMKT FVDQYGQRDD GKIGIVELAH VLPTEENFLL LFRCQQLKSC EEFMKTWRKY DTDHSGFIET EELKNFLKDL LEKANKTVDD TKLAEYTDLM LKLFDSNNDG KLELTEMARL LPVQENFLLK FQGIKMCGKE FNKAFELYDQ DGNGYIDENE LDALLKDLCE KNKQDLDINN ITTYKKNIMA LSDGGKLYRT DLALILCAGD N.
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.
- View Data Sheet
Name :
CAPZA2 HumanDescription:
Capping Protein (Actin Filament) Muscle Z-Line Alpha 2 Human Recombinant
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2, F-Actin Capping Protein Alpha-2 Subunit, CapZ Alpha-2, CAPPA, CAPZ2, F-Actin-Capping Protein Subunit Alpha-2.
Product # :
PRO-1721Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CAPZA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 309 amino acids (1-286 a.a) and having a molecular mass of 35.3kDa.CAPZA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CAPZA2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, and 0.4M UREA.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2 also known as CAPZA2 belongs the F-actin capping protein alpha subunit family. It is the alpha subunit of the barbed-end actin binding protein Cap Z. By capping the barbed end of actin filaments, Cap Z regulates the growth of the actin filaments at the barbed end. Among the diseases associated with CAPZA2 are endocarditis, and cervicitis.
-
Synonyms
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2, F-Actin Capping Protein Alpha-2 Subunit, CapZ Alpha-2, CAPPA, CAPZ2, F-Actin-Capping Protein Subunit Alpha-2.
-
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 MGSMADLEEQ LSDEEKVRIA AKFIIHAPPG EFNEVFNDVR LLLNNDNLLR EGAAHAFAQY NLDQFTPVKI EGYEDQVLIT EHGDLGNGKF LDPKNRICFK FDHLRKEATD PRPCEVENAV ESWRTSVETA LRAYVKEHYP NGVCTVYGKK IDGQQTIIAC IESHQFQAKN FWNGRWRSEW KFTITPSTTQ VVGILKIQVH YYEDGNVQLV SHKDIQDSLT VSNEVQTAKE FIKIVEAAEN EYQTAISENY QTMSDTTFKA LRRQLPVTRT KIDWNKILSY KIGKEMQNA.
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.
- View Data Sheet
Name :
KRT16 HumanDescription:
Cytokeratin 16 Human Recombinant
Keratin, type I cytoskeletal 16, Cytokeratin 16, KRT16, Cytokeratin-16, CK-16, Keratin-16, K16, KRT16A, FNEPPK, K1CP, NEPPK.
Product # :
PRO-1899Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
KRT16 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 496 amino acids (1-473) and having a molecular mass of 53.7 kDa.KRT16 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KRT16 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Cytokeratin 16, also known as KRT16, is a member of the keratin gene family. KRT16 which acts as a regulator of innate immunity in response to skin barrier breach is required for some inflammatory checkpoint for the skin barrier maintenance. KRT16 is coexpressed with keratin 14 in a few epithelial tissues as esophagus, tongue, and hair follicles.
-
Synonyms
Keratin, type I cytoskeletal 16, Cytokeratin 16, KRT16, Cytokeratin-16, CK-16, Keratin-16, K16, KRT16A, FNEPPK, K1CP, NEPPK.
-
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 MGSMTTCSRQ FTSSSSMKGS CGIGGGIGGG SSRISSVLAG GSCRAPSTYG GGLSVSSRFS SGGACGLGGG YGGGFSSSSS FGSGFGGGYG GGLGAGFGGG LGAGFGGGFA GGDGLLVGSE KVTMQNLNDR LASYLDKVRA LEEANADLEV KIRDWYQRQR PSEIKDYSPY FKTIEDLRNK IIAATIENAQ PILQIDNARL AADDFRTKYE HELALRQTVE ADVNGLRRVL DELTLARTDL EMQIEGLKEE LAYLRKNHEE EMLALRGQTG GDVNVEMDAA PGVDLSRILN EMRDQYEQMA EKNRRDAETW FLSKTEELNK EVASNSELVQ SSRSEVTELR RVLQGLEIEL QSQLSMKASL ENSLEETKGR YCMQLSQIQG LIGSVEEQLA QLRCEMEQQS QEYQILLDVK TRLEQEIATY RRLLEGEDAH LSSQQASGQS YSSREVFTSS SSSSSRQTRP ILKEQSSSSF SQGQSS.
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.
- View Data Sheet
Name :
GHRL HumanDescription:
Ghrelin Human Recombinant
Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.
Product # :
HOR-294Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Ghrelin Human Recombinant contains 115 amino acids (24-117 a.a.) and a total molecular mass of 12.8 kDa. The GHRL is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Ghrelin protein solution contains 20mM Tris-HCl, pH-8 & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Obestatin is a hormone that is produced in the cells lining the stomach and small intestine of several mammals including humans; it drastically reduces appetite in mice and is expected to do the same in humans. Obestatin is a peptide hormone - a relatively small protein. It is encoded by the same gene that also encodes ghrelin, a peptide hormone that increases appetite. The protein produced by that gene breaks into two smaller peptides, ghrelin and obestatin. Ghrelin is an endogenous ligand for the growth hormone secretagogue receptor and is involved in regulating growth hormone release. Ghrelin is derived from a preprohormone called preproghrelin, which also generates a second peptide called obestatin. Ghrelin is an endogenous ligand for the orphan G protein-coupled receptor GPR39 and is involved in satiety and decreased food intake.
-
Synonyms
Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.
-
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 MGSSFLSPEH QRVQQRKESK KPPAKLQPRA LAGWLRPEDG GQAEGAEDEM EVRFNAPFDV GIKLSGVQYQ QHSQALGKFL QDILWEEAKE APADK.
-
Background
What is the molecular weight/Mw of GHRELIN HUMAN Protein?
GHRELIN HUMAN Protein has a total Mw of 12.8kDa.
What is the source or expression system of GHRELIN HUMAN Protein?
Escherichia Coli.
What is the Purity of GHRELIN HUMAN Protein?
GHRELIN HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of GHRELIN HUMAN Protein?
The biological functionality of GHRELIN HUMAN Protein will be determined in the future.
What is the amino acid sequence of GHRELIN HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSSFLSPEH QRVQQRKESK KPPAKLQPRA LAGWLRPEDG GQAEGAEDEM EVRFNAPFDV GIKLSGVQYQ QHSQALGKFL QDILWEEAKE APADK.
What applications can GHRELIN HUMAN Protein be used in?
GHRELIN HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GHRELIN HUMAN Protein?
The endotoxin level is minimal, GHRELIN 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.
- View Data Sheet
Name :
TTC1 HumanDescription:
Tetratricopeptide Repeat Domain 1 Human Recombinant
Tetratricopeptide repeat protein 1, TPR repeat protein 1, TTC1, TPR1.
Product # :
PRO-1160Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TTC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-292 a.a) and having a molecular mass of 36.1kDa (Molecular weight on SDS-PAGE will appear higher).TTC1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TTC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
Tetratricopeptide repeat protein 1 (TTC1) is comprised of 292 amino acids with 3 TPR motifs, such as a Galpha16-binding protein. This interaction is confirmed both in vitro and in transfected mammalian cells, where TTC1 also binds to a number of other Galpha proteins. TTC1 interacts with Ha-Ras especially in its active form. TTC1 also interacts with the GAP domain of NF1.
-
Synonyms
Tetratricopeptide repeat protein 1, TPR repeat protein 1, TTC1, TPR1.
-
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 MGSHMGEKSE NCGVPEDLLN GLKVTDTQEA ECAGPPVPDP KNQHSQSKLL RDDEAHLQED QGEEECFHDC SASFEEEPGA DKVENKSNED VNSSELDEEY LIELEKNMSD EEKQKRREES TRLKEEGNEQ FKKGDYIEAE SSYSRALEMC PSCFQKERSI LFSNRAAARM KQDKKEMAIN DCSKAIQLNP SYIRAILRRA ELYEKTDKLD EALEDYKSIL EKDPSIHQAR EACMRLPKQI EERNERLKEE MLGKLKDLGN LVLRPFGLST ENFQIKQDSS TGSYSINFVQ NPNNNR.
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.
- View Data Sheet
Name :
CHRNA6 HumanDescription:
Cholinergic Receptor Nicotinic, Alpha 6 Human Recombinant
CHNRA6, Neuronal acetylcholine receptor subunit alpha-6, CHRNA6.
Product # :
PRO-1878Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CHRNA6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (26-239 a.a) and having a molecular mass of 29.3kDa. CHRNA6 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CHRNA6 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Cholinergic Receptor Nicotinic, Alpha 6 (CHRNA6) is a part of the nicotinic acetylcholine receptors (nAChRs) family. nAChRs are heteropentameric ligand-gated ion channels generating from the assembly of alpha and beta protein subunits. After binding acetylcholine, the AChRs respond by a major change in conformation which affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. CHRNA6 receptors have a rather selective localization to the nigrostriatal pathway.
-
Synonyms
CHNRA6, Neuronal acetylcholine receptor subunit alpha-6, CHRNA6.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSKGCV GCATEERLFH KLFSHYNQFI RPVENVSDPV TVHFEVAITQ LANVDEVNQI METNLWLRHI WNDYKLRWDP MEYDGIETLR VPADKIWKPD IVLYNNAVGD FQVEGKTKAL LKYNGMITWT PPAIFKSSCP MDITFFPFDH QNCSLKFGSW TYDKAEIDLL IIGSKVDMND FWENSEWEII DASGYKHDIK YNCCEEIYTD ITYSFYIRRL.
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.
- View Data Sheet
Name :
GREM1 HumanDescription:
GREM1 Human Recombinant
Gremlin-1 isoform 1, CKTSF1B1, DAND2, DRM, GREMLIN, IHG-2, PIG2, GREM1, Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 2.
Product # :
PRO-1359Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GREM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (25-184) and having a molecular mass of 20.7 kDa. GREM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GREM1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
GREM1 belongs to the BMP (bone morphogenic protein) antagonist family. Like BMPs, BMP antagonists comprise cystine knots and usually form homo- and heterodimers. The CAN (cerberus and dan) subfamily of BMP antagonists, to which GREM1 belongs, is characterized by a C-terminal cystine knot with an eight-membered ring. The antagonistic effect of the secreted glycosylated protein is because of its direct binding to BMP proteins. As an antagonist of BMP, GREM1 takes a place in regulating organogenesis, body patterning, and tissue differentiation. In mouse, GREM1 has been shown to convey the sonic hedgehog (SHH) signal from the polarizing region to the apical ectodermal ridge during limb bud outgrowth. Alternatively merged transcript variants encoding different isoforms have been found for this gene.
-
Synonyms
Gremlin-1 isoform 1, CKTSF1B1, DAND2, DRM, GREMLIN, IHG-2, PIG2, GREM1, Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 2.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSKKKGSQG AIPPPDKAQH NDSEQTQSPQ QPGSRNRGRG QGRGTAMPGE EVLESSQEAL HVTERKYLKR DWCKTQPLKQ TIHEEGCNSR TIINRFCYGQ CNSFYIPRHI RKEEGSFQSC SFCKPKKFTT MMVTLNCPEL QPPTKKKRVT RVKQCRCISI DLD.
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.
- View Data Sheet
Name :
CXCL1 HumanDescription:
GRO-Alpha Human Recombinant (CXCL1)
Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.
Product # :
CHM-329Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
GRO Alpha Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7811 Dalton. The GRO-alpha is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1mg/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
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.
More Info
-
Introduction
Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophilsand epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.
-
Synonyms
Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized GRO-alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL1 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 CXCL1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.
-
Background
What is the molecular weight/Mw of CXCL1 HUMAN Protein?
CXCL1 HUMAN Protein has a total Mw of 7.81kDa.
What is the source or expression system of CXCL1 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL1 HUMAN Protein?
CXCL1 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL1 HUMAN Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.
What is the amino acid sequence of CXCL1 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.
What applications can CXCL1 HUMAN Protein be used in?
CXCL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL1 HUMAN Protein?
The endotoxin level is minimal, CXCL1 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.
- View Data Sheet
Name :
CXCL3 Rat alphaDescription:
GRO-Gamma Rat Recombinant (CXCL3), CINC-2 alpha
Cytokine-induced neutrophil chemoattractant 2, CINC2, CINC-2, Macrophage inflammatory protein 2-alpha.
Product # :
CHM-258Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
GRO-g Rat Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7.8kDa. The CXCL3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Rat CXCL3 lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract 293 transfected CXCR2 cells using a concentration range of 10-100 ng/ml, corresponding to a specific activity of 10,000-100,000 units/mg.More Info
-
Introduction
Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.
-
Synonyms
Cytokine-induced neutrophil chemoattractant 2, CINC2, CINC-2, Macrophage inflammatory protein 2-alpha.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized GRO-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL3 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 GRO-gamma in sterile 18Mcm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
RELRCQCLKT LPRVDFENIQ SLTVTPPGPH CTQTEVIATL KDGQEVCLNP QAPRLQKIIQ KLLKSDKSS.
-
Background
What is the molecular weight/Mw of CXCL3 RAT ALPHA Protein?
CXCL3 RAT ALPHA Protein has a total Mw of 7.8kDa.
What is the source or expression system of CXCL3 RAT ALPHA Protein?
Escherichia Coli.
What is the Purity of CXCL3 RAT ALPHA Protein?
CXCL3 RAT ALPHA Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL3 RAT ALPHA Protein?
Determined by its ability to chemoattract 293 transfected CXCR2 cells using a concentration range of 10-100 ng/ml, corresponding to a specific activity of 10,000-100,000 units/mg.
What is the amino acid sequence of CXCL3 RAT ALPHA Protein?
RELRCQCLKT LPRVDFENIQ SLTVTPPGPH CTQTEVIATL KDGQEVCLNP QAPRLQKIIQ KLLKSDKSS.
What applications can CXCL3 RAT ALPHA Protein be used in?
CXCL3 RAT ALPHA Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL3 RAT ALPHA Protein?
The endotoxin level is minimal, CXCL3 RAT ALPHA 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.
- View Data Sheet
Name :
CCL12 MouseDescription:
Monocyte Chemotactic Protein-5 Mouse Recombinant (CCL12)
C-C motif chemokine 12, MCP-1-related chemokine, Monocyte chemoattractant protein 5, Monocyte chemotactic protein 5, MCP-5, Small-inducible cytokine A12, Ccl12, Mcp5, Scya12.
Product # :
CHM-266Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
MCP-5 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 82 amino acids and having a molecular mass of 9.3kDa. The MCP5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human peripheral blood monocytes using a concentration range of 10.0-50.0 ng/ml.More Info
-
Introduction
MCP-5 (CCL12) is a cloned mouse CC chemokine most closely related to human MCP1 (66% amino acid sequence identity in the mature protein). MCP5 is expressed constitutively in the thymus and the lymph nodes. Under inflammatory conditions, moreover CCL12 expression is induced in activated macrophages and mast cells. The mouse MCP1 gene is mapped to the CC chemokine cluster on chromosome 11. Recombinant CCL12 is a potent chemoattractant for monocytes and lymphocytes but not neutrophils. At high concentrations, MCP-5 also chemoattracts eosinophils. CCL12 is a functional ligand for CCR2.
-
Synonyms
C-C motif chemokine 12, MCP-1-related chemokine, Monocyte chemoattractant protein 5, Monocyte chemotactic protein 5, MCP-5, Small-inducible cytokine A12, Ccl12, Mcp5, Scya12.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized CCL12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCP5 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 MCP5 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
GPDAVSTPVT CCYNVVKQKI HVRKLKSYRR ITSSQCPREA VIFRTILDKE ICADPKEKWV KNSINHLDKT SQTFILEPSC LG.
-
Background
What is the molecular weight/Mw of CCL12 MOUSE Protein?
CCL12 MOUSE Protein has a total Mw of 9.3kDa.
What is the source or expression system of CCL12 MOUSE Protein?
Escherichia Coli.
What is the Purity of CCL12 MOUSE Protein?
CCL12 MOUSE Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL12 MOUSE Protein?
Determined by its ability to chemoattract human peripheral blood monocytes using a concentration range of 10.0-50.0 ng/ml.
What is the amino acid sequence of CCL12 MOUSE Protein?
GPDAVSTPVT CCYNVVKQKI HVRKLKSYRR ITSSQCPREA VIFRTILDKE ICADPKEKWV KNSINHLDKT SQTFILEPSC LG.
What applications can CCL12 MOUSE Protein be used in?
CCL12 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL12 MOUSE Protein?
The endotoxin level is minimal, CCL12 MOUSE 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.
- View Data Sheet
Name :
SSTDescription:
Somatostatin
Growth hormone release-inhibiting factor, SST, SMS, SMST, GHIH.
Product # :
HOR-299Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
Somatostatin Synthetic is a single, non-glycosylated polypeptide chain containing 14 amino acids, having a molecular mass of 1637.9 Dalton and a Molecular formula of C76H104N18O19S2. The CAS# is 38916-34-6.
Formulation
The protein 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
Somatostatin (also known as growth hormone inhibiting hormone (GHIH) or somatotropin release-inhibiting hormone (SRIF) is a peptide hormone that regulates the endocrine systemand affects neurotransmission and cell proliferation via interaction with G-protein-coupled somatostatin receptors and inhibition of the release of numerous secondary hormones. Somatostatin has two active forms produced by alternative cleavage of a single preproprotein: one of 14 amino acids, the other of 28 amino acids.
-
Synonyms
Growth hormone release-inhibiting factor, SST, SMS, SMST, GHIH.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized SST although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Somatostatin 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 Somatostatin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
Ala-Gly-Cys-Lys-Asn-Phe- Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys-OH.
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.
- View Data Sheet
Name :
IL1A Human, His ActiveDescription:
Interleukin-1 alpha Human Recombinant, His Tag Active
Interleukin-1 alpha, IL-1 alpha, Hematopoietin-1, Interleukin-1 alpha: Interleukin-1a, IL-1a, Interleukin-1 alpha, IL1A, interleukin 1 alpha, IL1F1, IL-1A, preinterleukin 1 alpha, pro-interleukin-1-alpha.
Product # :
CYT-1134Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
IL1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (113-271 a.a) and having a molecular mass of 22.4kDa. IL1A is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
IL1A protein solution (1mg/ml) contains 20mM Tris-HCl (pH 7.5) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using D10.G4.1 mouse helper T cell. The ED50 for this effect is less or equal to 0.04 ng/ml.
More Info
-
Introduction
IL-1 alpha is derived fromactivated macrophages. IL1A proteins take part in the inflammatory response, being identified as endogenous pyrogens, and stimulate the release of prostaglandin and collagenase from synovial cells.IL-1 alpha stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity.
-
Synonyms
Interleukin-1 alpha, IL-1 alpha, Hematopoietin-1, Interleukin-1 alpha: Interleukin-1a, IL-1a, Interleukin-1 alpha, IL1A, interleukin 1 alpha, IL1F1, IL-1A, preinterleukin 1 alpha, pro-interleukin-1-alpha.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMSA PFSFLSNVKY NFMRIIKYEF ILNDALNQSI IRANDQYLTA AALHNLDEAV KFDMGAYKSS KDDAKITVIL RISKTQLYVT AQDEDQPVLL KEMPEIPKTI TGSETNLLFF WETHGTKNYF TSVAHPNLFI ATKQDYWVCL AGGPPSITDF QILENQA.
-
Background
What is the molecular weight/Mw of IL1A HUMAN, HIS ACTIVE Protein?
IL1A HUMAN, HIS ACTIVE Protein has a total Mw of 22.4kDa.
What is the source or expression system of IL1A HUMAN, HIS ACTIVE Protein?
Escherichia Coli.
What is the Purity of IL1A HUMAN, HIS ACTIVE Protein?
IL1A HUMAN, HIS ACTIVE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IL1A HUMAN, HIS ACTIVE Protein?
Measured in a cell proliferation assay using D10.G4.1 mouse helper T cell. The ED50 for this effect is less or equal to 0.04 ng/ml.
What is the amino acid sequence of IL1A HUMAN, HIS ACTIVE Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMSA PFSFLSNVKY NFMRIIKYEF ILNDALNQSI IRANDQYLTA AALHNLDEAV KFDMGAYKSS KDDAKITVIL RISKTQLYVT AQDEDQPVLL KEMPEIPKTI TGSETNLLFF WETHGTKNYF TSVAHPNLFI ATKQDYWVCL AGGPPSITDF QILENQA.
What applications can IL1A HUMAN, HIS ACTIVE Protein be used in?
IL1A HUMAN, HIS ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL1A HUMAN, HIS ACTIVE Protein?
The endotoxin level is minimal, IL1A HUMAN, HIS ACTIVE 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.
- View Data Sheet
Name :
AlarelinDescription:
Alarelin
Alarelin, Alarelin Acetate.
Product # :
HOR-291Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
Alarelin acetate peptide is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 1167.3 Dalton and a Molecular formula of C56H78N16O12 x C2H4O2. The CAS No. is 79561-22-1.
Formulation
The Alarelin was lyophilized with no additives.
Purity
Greater than 99.0% as determined by Analysis by RP-HPLC.
More Info
-
Introduction
Alarelin (Gonadotrophin-releasing hormone) is a synthetic LH-RH agonist that is found in higher amounts than that of LH-RH in rat hypophyseal stimulation of gonadotropin secretion in vivo and in vitro and in ovulation inductions. Alarelin is known for its induction of ovulation. Alarelin acetate is the acetate form of a hypothalamic peptide that stimulates the release of FSH and LH from the pituitary gland.
-
Synonyms
Alarelin, Alarelin Acetate.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Alarelin e although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Alarelin 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 Argipressin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
5-oxo-pro-His-Trp-Ser-Tyr-D-Ala-Leu-Arg-Pro-Nhet x CH3COOH.
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.
- View Data Sheet
Name :
AK1 MouseDescription:
Adenylate Kinase 1 Mouse Recombinant
Adenylate kinase Isoenzyme 1 isoform 1, Ak-1, B430205N08Rik, ATP-AMP transphosphorylase 1, ATP:AMP phosphotransferase, Adenylate monophosphate kinase, Myokinase.
Product # :
PKA-106Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
AK1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a) and having a molecular mass of 25.5kDa.AK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AK1 protein solution (0.5mg/ml) containing 20mM Tris-Hcl buffer (pH8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 150 units/mg. One unit will convert 2.0 umoles of ADP to ATP + AMP per minute at pH 7.5 at 37C.
More Info
-
Introduction
AK1 is a small ubiquitous enzyme which is essential for maintenance and cell growth. It is involved in the regulation of adenine nucleotide composition within a cell by catalyzing the reversible transfer of the terminal phosphate group between ATP and AMP. The AK1 protein is found in the cytosol of skeletal muscle, brain and erythrocytes. Defects in the AK1 gene are the cause of a form of hemolytic anemia.
-
Synonyms
Adenylate kinase Isoenzyme 1 isoform 1, Ak-1, B430205N08Rik, ATP-AMP transphosphorylase 1, ATP:AMP phosphotransferase, Adenylate monophosphate kinase, Myokinase.
-
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 MGSMGCCVSS EPQEEGGRKT GEKLKKAKII FVVGGPGSGK GTQCEKIVQK YGYTHLSTGD LLRAEVSSGS ERGKKLSAIM EKGELVPLDT VLDMLRDAML AKVDSSNGFL IDGYPREVKQ GEEFEQKIGQ PTLLLYVDAG AETMTQRLLK RGETSGRVDD
NEETIKKRLE TYYNATEPVI SFYDKRGIVR KVNAEGTVDT VFSEVCTYLD SLK.
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.