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1000 results found for “cofilin”
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Name :
CCL24 RatDescription:
Eotaxin-2 Rat Recombinant (CCL24)
C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.
Product # :
CHM-282Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CCL24 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of 10.2kDa. The CCL24 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 murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
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Introduction
Eotaxin-2, also called MPIF2 & Ckb6, is a novel CC chemokine produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Furthermore, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which includes C-terminal truncation, contains 78 amino acids (92 amino acids for the mouse homolog, without C-terminal truncation).
CCL24 functions as a chemotactic chemokine for resting t-lymphocytes, and eosinophils. CCL24 has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. CCL24 is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line and binds to CCR3. -
Synonyms
C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Eotaxin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL24 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.
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Solubility
It is recommended to reconstitute the lyophilized CCL24 Rat Recombinant in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
VTIPSSCCVT FISKKIPVNR VISYQLANGS ICPKAGVIFI TKKGHKICTD PKLPWVQKHI KNLDAKRNQP SEGAKALGPK FVIQKLRGNS TKV.
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Background
What is the molecular weight/Mw of CCL24 RAT Protein?
CCL24 RAT Protein has a total Mw of 10.2kDa.
What is the source or expression system of CCL24 RAT Protein?
Escherichia Coli.
What is the Purity of CCL24 RAT Protein?
CCL24 RAT Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL24 RAT Protein?
Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CCL24 RAT Protein?
VTIPSSCCVT FISKKIPVNR VISYQLANGS ICPKAGVIFI TKKGHKICTD PKLPWVQKHI KNLDAKRNQP SEGAKALGPK FVIQKLRGNS TKV.
What applications can CCL24 RAT Protein be used in?
CCL24 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL24 RAT Protein?
The endotoxin level is minimal, CCL24 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.
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Name :
NEFL HumanDescription:
Neurofilament Light Human Recombinant
Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.
Product # :
PRO-2584Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
NEFL Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (2-543 a.a) containing 551 amino acids including a 9 a.a N-terminal His tag. The total molecular mass is 62.5kDa (calculated).
Source
Escherichia Coli.
Formulation
NEFL filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in 15mM Tris and 85mM Glycine, pH 8.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
NEFL or Neurofilament light polypeptide is a protein that is encoded through the NEFL gene. NEFL is correlated to a disease called Charcot–Marie–Tooth. The protein’s light subunit is determined by immunoassays in the plasma and cerebrospinal fluid, if present, it can indicate on axonal damage in neurological diseases. By doing so, NEFL can act as a marker for Huntington's disease, Amyotrophic Lateral Sclerosis and multiple sclerosis.
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Synonyms
Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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.
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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.
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Amino Acid Sequence
MKHHHHHHAS SFSYEPYYST SYKRRYVETP RVHISSVRSG YSTARSAYSS YSAPVSSSLS VRRSYSSSSG SLMPSLENLD LSQVAAISND LKSIRTQEKA QLQDLNDRFA SFIERVHELE QQNKVLEAEL LVLRQKHSEP SRFRALYEQE IRDLRLAAED ATNEKQALQG EREGLEETLR NLQARYEEEV LSREDAEGRL MEARKGADEA ALARAELEKR IDSLMDEISF LKKVHEEEIA ELQAQIQYAQ ISVEMDVTKP DLSAALKDIR AQYEKLAAKN MQNAEEWFKS RFTVLTESAA KNTDAVRAAK DEVSESRRLL KAKTLEIEAC RGMNEALEKQ LQELEDKQNA DISAMQDTIN KLENELRTTK SEMARYLKEY QDLLNVKMAL DIEIAAYRKL LEGEETRLSF TSVGSITSGY SQSSQVFGRS AYGGLQTSSY LMSTRSFPSY YTSHVQEEQI EVEETIEAAK AEEAKDEPPS EGEAEEEEKD KEEAEEEEAA EEEEAAKEES EEAKEEEEGG EGEEGEETKE AEEEEKKVEG AGEEQAAKKK D.
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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Name :
CFI HumanDescription:
Complement Factor I Human
Complement factor I, C3B/C4B inactivator, CFI, IF.
Product # :
PRO-2701Price :
Quantity :
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Description
Human Complement Factor I produced in Human plasma is glycosylated polypeptide composed of 2 disulfide-linked chains having a total molecular mass of 88kDa.
Source
Human Plasma.
Formulation
CFI protein solution contains Sodium phosphate, pH 7.2.
Purity
Greater than 93.0% as determined by SDS-PAGE.
More Info
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Introduction
CFI cleaves and inactivates C3b and C4b. CFI is inactive without a cofactor such as the soluble factor H and C4b binding protein. CFI cleaves the alpha-peptide chain of C3b and C4b when these binds1 of the cofactors. This cleavage inactivates all of the complement activating functions of these proteins producing iC3b and iC4b.CFI cleaves the alpha chain of C3b twice and this releases a small fragment called C3f. CFI can cleave iC3b releasing C3c from C3dg in the presence of CR1.C4b is cleaved rapidly at 2 sites separating C4c from C4d.
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Synonyms
Complement factor I, C3B/C4B inactivator, CFI, IF.
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Physical Appearance
Sterile filtered solution.
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Stability
CFI Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.
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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.
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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Name :
BLyS HumanDescription:
B-cell Activating Factor Human Recombinant
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
Product # :
CYT-307Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
BAFF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids and having a molecular mass of 17007 Dalton. The BAFF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.0.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by a mouse splenocyte survival assay. The ED50 for this effect is 0.5-2.0µg/ml.More Info
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Introduction
BAFF binds to tnfrsf13b/taci and tnfrsf17/bcma. Tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity. A third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin. -
Synonyms
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BAFF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BAFF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized BAFF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MAVQGPEETV TQDCLQLIAD SETPTIQKGS YTFVPWLLSF KRGSALEEKE NKILVKETGY FFIYGQVLYT DKTYAMGHLI QRKKVHVFGD ELSLVTLFRC IQNMPETLPN NSCYSAGIAK LEEGDELQLA IPRENAQISL DGDVTFFGAL KLL.
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Background
What is the molecular weight/Mw of BLYS Protein?
BLYS Protein has a total Mw of 17.7kDa.
What is the source or expression system of BLYS Protein?
Escherichia Coli.
What is the Purity of BLYS Protein?
BLYS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BLYS Protein?
The activity is determined by a mouse splenocyte survival assay. The ED50 for this effect is 0.5-2.0µg/ml.
What is the amino acid sequence of BLYS Protein?
MAVQGPEETV TQDCLQLIAD SETPTIQKGS YTFVPWLLSF KRGSALEEKE NKILVKETGY FFIYGQVLYT DKTYAMGHLI QRKKVHVFGD ELSLVTLFRC IQNMPETLPN NSCYSAGIAK LEEGDELQLA IPRENAQISL DGDVTFFGAL KLL.
What applications can BLYS Protein be used in?
BLYS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BLYS Protein?
The endotoxin level is minimal, BLYS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PIN1 MouseDescription:
Peptidyl-Prolyl Cis/Trans Isomerase NIMA-Interacting 1 Mouse Recombinant
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC:5.2.1.8), Peptidyl-prolyl cis-trans isomerase Pin1, PPIase Pin1, Pin1, PIN1.
Product # :
ENZ-1045Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PIN1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-165 a.a) and having a molecular mass of 20.8kDa. PIN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PIN1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 1,200 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAFP-PNA per minute at 37°C in Tris-HCl pH 8.0 using chymotrypsin.
More Info
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Introduction
Pin 1 is a peptidyl-prolyl cis/trans isomerase (PPIase) which interacts with NIMA and essential for cell cycle regulation Pin1 is nuclear PPIase containing a WW protein interaction domain, and is structurally and functionally related to Ess1/Ptf1, an essential protein in budding yeast. PPIase activity is necessary for Ess1/Pin1 function in yeast. Pin1 is thus an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Substrates of Pin1 include the mitotic regulators (Cdc25 phosphatase and NIMA, PLK I, Wee, and Myt1 kinases), several transcription factors like b-Catenin, c-Jun, and the tumor suppressor protein p53, and some specific proteins like the RNA Pol II, the cytoskeleton protein tau, and the G1/S protein Cyclin D1.
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Synonyms
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC:5.2.1.8), Peptidyl-prolyl cis-trans isomerase Pin1, PPIase Pin1, Pin1, PIN1.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMADEEKL PPGWEKRMSR SSGRVYYFNH ITNASQWERP SGGSTVGGSS KNGQGEPAKV RCSHLLVKHS QSRRPSSWRQ EKITRSKEEA LELINGYIQK IKSGEEDFES LASQFSDCSS AKARGDLGPF SRGQMQKPFE DASFALRTGE MSGPVFTDSG IHIILRTE.
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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Name :
PPIH Human, HisDescription:
Cyclophilin-H Human Recombinant, His Tag
Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.
Product # :
ENZ-730Price :
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Shipping Method :
Shipped at Room temp
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Description
PPIH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 2-177) containing 186 amino acids and including a 10 a.a N-terminal His tag. The total molecular mass is 20.3kDa (calculated).
Source
Escherichia Coli.
Formulation
Filtered (0.4 µm) and lyophilized from 0.5 mg/ml in phosphate buffered saline pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PPIH is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and increase protein folding. PPIH enzyme is a precise factor of the complex that comprises pre-mRNA processing factors PRPF3, PRPF4, and PRPF18, as well as U4/U5/U6 tri-snRNP. PPIH possess PPIase activity and acts as a protein chaperone that mediates the interactions between different proteins inside the spliceosome.
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Synonyms
Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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.
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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. PPIH is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASAVANSSPVNP VVFFDVSIGG QEVGRMKIEL FADVVPKTAE NFRQFCTGEF RKDGVPIGYK GSTFHRVIKD FMIQGGDFVN GDGTGVASIY RGPFADENFK LRHSAPGLLS MANSGPSTNG CQFFITCSKC DWLDGKHVVF GKIIDGLLVM RKIENVPTGP NNKPKLPVVI SQCGEM.
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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Name :
SCF HumanDescription:
Stem Cell Factor Human Recombinant
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.
Product # :
CYT-255Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Stem Cell Factor Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids and having a molecular mass of 18409 Dalton. The SCF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of Human TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000 IU/mg.More Info
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Introduction
Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117(c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases. SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).
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Synonyms
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized KIT ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF 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.
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Solubility
It is recommended to reconstitute the lyophilized Stem Cell Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Glu-Gly-Ile-Cys.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.52 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 Stem Cell Factor 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.
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Name :
NAIF1 HumanDescription:
Nuclear Apoptosis Inducing Factor 1 Human Recombinant
bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.
Product # :
PRO-1978Price :
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Shipping Method :
Shipped with Ice Packs
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Description
NAIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (1-327 a.a) and having a molecular mass of 37.6kDa. NAIF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NAIF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Nuclear Apoptosis Inducing Factor 1 (NAIF1) is a part of the NAIF1 family. NAIF1 Interacts with HARBI1 and Induces apoptosis.
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Synonyms
bA379C10.2, C9orf90, RP11-379C10.2, Nuclear apoptosis-inducing factor 1, NAIF1.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAVPAKK RKMNFSEREV EIIVEELELK KHLLVNHFNA GVPLAAKSAA WHGILRRVNA VATCRRELPE VKKKWSDLKT EVRRKVAQVR AAVEGGEAPG PTEEDGAGGP GTGGGSGGGG PAVAPVLLTP MQQRICNLLG EATIISLPST TEIHPVALGP SATAAAATVT LTQIPTETTY HTLEEGVVEY CTAEAPPPLP PETPVDMMAQ HADTSVKPQA LKSRIALNSA KLIQEQRVTN LHVKEIAQHL EQQNDLLQMI RRSQEVQACA QERQAQAMEG TQAALSVLIQ VLRPMIKDFR RYLQSNTANP APASDPGQVA QNGQPDSIIQ.
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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Name :
COPE HumanDescription:
Coatomer Protein Complex Subunit Epsilon Human Recombinant
Coatomer Protein Complex, Subunit Epsilon, Epsilon-Coat Protein, Epsilon-COP, Coatomer Epsilon Subunit, Coatomer Subunit Epsilon, Epsilon Coat Protein, Coatomer subunit epsilon.
Product # :
PRO-2120Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
COPE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-308 a.a) and having a molecular mass of 36.9kDa. COPE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
COPE protein solution (0.25 mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Coatomer Protein Complex SubunitEpsilon, also known as COPE is an epsilon subunit of coatomer protein complex. Coatomer is a cytosolic protein complex which binds to dilysine motifs and reversibly links with Golgi non-clathrin-coated vesicles. COPE is necessary forbudding from Golgi membranes, and is also essential for the retrograde Golgi-to-ER transport of dilysine-taggedproteins. Coatomer complex contain at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Alternatively spliced transcript variants encoding dissimilar isoforms have been identifiedfor COPE.
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Synonyms
Coatomer Protein Complex, Subunit Epsilon, Epsilon-Coat Protein, Epsilon-COP, Coatomer Epsilon Subunit, Coatomer Subunit Epsilon, Epsilon Coat Protein, Coatomer subunit epsilon.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAPPAPG PASGGSGEVD ELFDVKNAFY IGSYQQCINE AQRVKLSSPE RDVERDVFLY RAYLAQRKFG VVLDEIKPSS APELQAVRMF ADYLAHESRR DSIVAELDRE MSRSVDVTNT TFLLMAASIY LHDQNPDAAL RALHQGDSLE CTAMTVQILL KLDRLDLARK ELKRMQDLDE DATLTQLATA WVSLATGGEK LQDAYYIFQE MADKCSPTLL LLNGQAACHM AQGRWEAAEG LLQEALDKDS GYPETLVNLI VLSQHLGKPP EVTNRYLSQL KDAHRSHPFI KEYQAKENDF DRLVLQYAPS A.
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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Name :
CFD HumanDescription:
Complement Factor D Human
Complement factor D, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD.
Product # :
PRO-2699Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Human Complement Factor D produced in Human plasma is glycosylated polypeptide chain having a total molecular mass of 24kDa.
Source
Human Plasma.
Formulation
CFD protein solution contains 10mM Sodium phosphate and 145mM NaCl, pH 7.3.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CFD is an important component of the alternative pathway of complement activation. CFD cleaves and activates factor B when it binds C3b or a C3b-like protein such as C3 or CVF. CFD is a serine protease that exists as a mature protease, but it exhibits a highly restricted specificity and it appears to be substrate activated. CFD cleaves factor B bound to C3b leading to the release of the Ba fragment and leaving the Bb fragment bound to C3b. The C3b,Bb complex is called a C3 or C5 convertase because it converts these proteins to their active forms by cleaving off the small peptides C3a and C5a, respectively.
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Synonyms
Complement factor D, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD.
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Physical Appearance
Sterile filtered solution.
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Stability
CFD Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.
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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.
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 :
FlagellinDescription:
Flagellin Recombinant
Product # :
PRO-1240Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Flagellin Salmonella typhimurium Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 503 amino acids with Leu, Glu and a 6 × His at C-terminus and having a molecular mass of 52.7kDa.The Flagellin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2um filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
More Info
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Introduction
Flagellin arranges itself in a hollow cylinder to create the filament in bacterial flagellum. Flagellin is the key substituent of bacterial flagellum, and is found in large quantities on almost all flagellated bacteria.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Flagellin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flagellin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Flagellin in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MAQVINTNSL SLLTQNNLNK SQSALGTAIE RLSSGLRINS AKDDAAGQAI ANRFTANIKG LTQASRNAND GISIAQTTEG ALNEINNNLQ RVRELAVQSA NSTNSQSDLD SIQAEITQRL NEIDRVSGQT QFNGVKVLAQ DNTLTIQVGA NDGETIDIDL KQINSQTLGL DTLNVQQKYK VSDTAATVTG YADTTIALDN STFKASATGL GGTDQKIDGD LKFDDTTGKY YAKVTVTGGT GKDGYYEVSV DKTNGEVTLA GGATSPLTGG LPATATEDVK NVQVANADLT EAKAALTAAG VTGTASVVKM SYTDNNGKTI DGGLAVKVGD DYYSATQNKD GSISINTTKY TADDGTSKTA LNKLGGADGK TEVVSIGGKT YAASKAEGHN FKAQPDLAEA AATTTENPLQ KIDAALAQVD TLRSDLGAVQ NRFNSAITNL GNTVNNLTSA RSRIEDSDYA TEVSNMSRAQ ILQQAGTSVL AQANQVPQNV LSLLRLEHHH 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.
- View Data Sheet
Name :
PFDN2 HumanDescription:
Prefoldin Subunit 2 Human Recombinant
Prefoldin subunit 2, PFDN2, PFD2.
Product # :
PRO-001Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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- formulation
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Description
PFDN2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids (1-154 a.a.) and having a molecular mass of 18.8kDa. The PFDN2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PFDN2 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 50mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Prefoldin subunit 2 (PFDN2) belongs to the prefoldin beta subunit family. The PFDN2 protein is one of 6 subunits of prefoldin, which is a molecular chaperone complex that binds and stabilizes newly synthesized polypeptides, thus allowing them to fold correctly. PFDN2 binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. PFDN2 also binds to a nascent polypeptide chain and promotes folding in an setting in which there are many competing pathways for nonnative proteins.
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Synonyms
Prefoldin subunit 2, PFDN2, PFD2.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAENSGRAGK SSGSGAGKGA VSAEQVIAGF NRLRQEQRGL ASKAAELEME LNEHSLVIDT LKEVDETRKC YRMVGGVLVE RTVKEVLPAL ENNKEQIQKI IETLTQQLQA KGKELNEFRE KHNIRLMGED EKPAAKENSE GAGAKASSAG VLVS.
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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Name :
CFH HumanDescription:
Complement Factor H Human
Complement factor H, H factor 1, CFH, HF, HF1, HF2.
Product # :
PRO-2700Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
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Description
Human Complement Factor H produced in Human plasma having a total molecular mass of 155kDa.
Source
Human Plasma.
Formulation
CFH protein solution contains PBS, pH 7.2.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Complement factor H (CFH) is an important regulatory component of the alternative pathway of complement. CFH is prevents complement activation on host cells and tissues, mainly the kidney. CFH controls the formation and decay of the alternative pathway C3/C5 convertase and acts as a cofactor for factor I which proteolytically inactivates C3b when C3b is bound to factor H. The N-terminal 5 domains of CFH bind to C3b and inhibit binding of factor B thus reducing the formation of C3/C5 convertase. CFH also binds to preformed C3/C5 convertases and causes quick release of the catalytic subunit Bb. These activities are necessary for controlling the spontaneous activation of the alternative pathway amplification process in plasma. In addition, CFH controls the formation and decay of these enzymes when C3b is attached to the surface of particles.
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Synonyms
Complement factor H, H factor 1, CFH, HF, HF1, HF2.
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Physical Appearance
Sterile filtered solution.
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Stability
CFH Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.
-
Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.
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 :
ITAC (63-87) HumanDescription:
ITAC (63-87 a.a.) Human Recombinant
ITAC, I-TAC, CXCL-11, CXCL11.
Product # :
CHM-049Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- More Info
Description
The I-TAC Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The I-TAC His-Tagged Fusion Protein, produced in E. coli, is a 9kDa protein containing 25 amino acid residues of the I-TACHuman, 63-87 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
ITAC, I-TAC, CXCL-11, CXCL11.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized I-TAC 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.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
I-TAC is a small cytokine belongs to the CXC chemokinen family which also called inducible T-cell alpha chemoattractant and IP-9. I-TAC is expressed mainly in peripheral blood leukocytes, liver and pancreas with moderate levels in spleen, thymus and lung and low levels in small intestine, placenta and prostate. IFN-g and IFN-b induces strongly gene expression of I-TAC. The I-TAC chemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10.
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 :
Platelet Factor 4 BovineDescription:
Platelet Factor-4 (CXCL4) Bovine Recombinant
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Product # :
CHM-039Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Platelet Factor-4 (CXCL4) Bovine Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 88 amino acid and having a molecular mass of approximately 9.5kDa.PF4 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 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity determined by a chemotaxis bioassay using human neutrophils is 10-100ng/ml.
More Info
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Introduction
Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets.PF4’s major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemokine family. Furthermore, it is used as an inhibitor in the angiogenesis during tumor therapy.
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Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Platelet Factor-4 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Platelet Factor-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ESSFPATFVP LPADSEGGED EDLQCVCLKT TSGINPRHIS SLEVIGAGTH CPSPQLLATK KTGRKICLDQ QRPLYKKILK KLLDGDES.
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Background
What is the molecular weight/Mw of PLATELET FACTOR 4 BOVINE Protein?
PLATELET FACTOR 4 BOVINE Protein has a total Mw of 9.5kDa.
What is the source or expression system of PLATELET FACTOR 4 BOVINE Protein?
Escherichia Coli.
What is the Purity of PLATELET FACTOR 4 BOVINE Protein?
PLATELET FACTOR 4 BOVINE Protein is > 95% pure as determined by SDS-PAGE.
What is the Biological Activity of PLATELET FACTOR 4 BOVINE Protein?
The biological activity determined by a chemotaxis bioassay using human neutrophils is 10-100ng/ml.
What is the amino acid sequence of PLATELET FACTOR 4 BOVINE Protein?
ESSFPATFVP LPADSEGGED EDLQCVCLKT TSGINPRHIS SLEVIGAGTH CPSPQLLATK KTGRKICLDQ QRPLYKKILK KLLDGDES.
What applications can PLATELET FACTOR 4 BOVINE Protein be used in?
PLATELET FACTOR 4 BOVINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for PLATELET FACTOR 4 BOVINE Protein?
The endotoxin level is minimal, PLATELET FACTOR 4 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.
- View Data Sheet
Name :
HPCAL1 HumanDescription:
Hippocalcin-Like 1 Human Recombinant
Hippocalcin-Like 1, HLP2, BDR1, Calcium-Binding protein BDR-1, Visinin-Like protein 3, VILIP-3
Product # :
PRO-254Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
HPCAL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213amino acids (1-193a.a.) and having a molecular wieght of 24.4kDa. The HPCAL1 is fused to 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HPCAL1 protein solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0) containing 1mM DTT 0.2M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
HPCAL1, participates in neuron-specific calcium-binding proteins family found in the retina and brain. HPCAL1 is extremely comparable to human hippocalcin protein and almost equal to the rat and mouse hippocalcin like-1 proteins. HPCAL1 takes part in the calcium-dependent regulation of rhodopsin phosphorylation and can have importance in neuronal signalling in the central nervous system.
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Synonyms
Hippocalcin-Like 1, HLP2, BDR1, Calcium-Binding protein BDR-1, Visinin-Like protein 3,
VILIP-3 -
Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGKQNSKLRP EVLQDLRENT EFTDHELQEW YKGFLKDCPT GHLTVDEFKK IYANFFPYGD ASKFAEHVFR TFDTNGDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISRSE MLEIVQAIYK MVSSVMKMPE DESTPEKRTD KIFRQMDTNN DGKLSLEEFI RGAKSDPSIV RLLQCDPSSA SQF
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 :
TIPIN HumanDescription:
TIMELESS Interacting Protein Human Recombinant
TIMELESS Interacting Protein, CSM3 Homolog.
Product # :
PRO-1710Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TIPIN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (1-301) and having a molecular mass of 36.9kDa.TIPIN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TIPIN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
TIPIN is a member of the CSM3 family. TIPIN protein is essential for normal advancement of S-phase and vital for cell existence after DNA damage or replication stress. TIPIN is specifically necessary for the ATR - CHEK1 pathway in the replication checkpoint induced by ultraviolet light.
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Synonyms
TIMELESS Interacting Protein, CSM3 Homolog.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMLEPQEN GVIDLPDYEH VEDETFPPFP PPASPERQDG EGTEPDEESG NGAPVPVPPK RTVKRNIPKL DAQRLISERG LPALRHVFDK AKFKGKGHEA EDLKMLIRHM EHWAHRLFPK LQFEDFIDRV EYLGSKKEVQ TCLKRIRLDL PILHEDFVSN NDEVAENNEH DVTSTELDPF LTNLSESEMF ASELSRSLTE EQQQRIERNK QLALERRQAK LLSNSQTLGN DMLMNTPRAH TVEEVNTDED QKEESNGLNE DILDNPCNDA IANTLNEEET LLDQSFKNVQ QQLDATSRNI TEAR
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 :
PPIL4 HumanDescription:
Peptidylprolyl Isomerase (Cyclophilin)-Like 4 Human Recombinant
Peptidyl-prolyl cis-trans isomerase-like 4, PPIase, Cyclophilin-like protein PPIL4, Rotamase PPIL4, PPIL4, HDCME13P.
Product # :
ENZ-026Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
PPIL4 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 512 amino acids (1-492 a.a.) and having a molecular mass of 59.3kDa. The PPIL4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PPIL solution (0.5 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 190 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.More Info
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Introduction
PPIL4 belongs to an evolutionarily conserved cyclophilin-type PPIase family of proteins. PPIL4, which is ubiquitously expressed with predominant expression in kidney localizes to the nucleus and contains one PPIase cyclophilin-type domain, a lysine-rich domain, a pair of bipartite nuclear targeting sequences and one RRM (RNA recognition motif) domain. The presence of the RRM domain along with nuclear targeting sequences implies that PPIL4 may be involved in transcriptional regulation.
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Synonyms
Peptidyl-prolyl cis-trans isomerase-like 4, PPIase, Cyclophilin-like protein PPIL4, Rotamase PPIL4, PPIL4, HDCME13P.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAVLLETTLG DVVIDLYTEE RPRACLNFLK LCKIKYYNYC LIHNVQRDFI IQTGDPTGTG RGGESIFGQL YGDQASFFEA EKVPRIKHKK KGTVSMVNNG SDQHGSQFLI TTGENLDYLD GVHTVFGEVT EGMDIIKKIN ETFVDKDFVP YQDIRINHTV ILDDPFDDPP DLLIPDRSPE PTREQLDSGR IGADEEIDDF KGRSAEEVEE IKAEKEAKTQ AILLEMVGDL PDADIKPPEN VLFVCKLNPV TTDEDLEIIF SRFGPIRSCE VIRDWKTGES LCYAFIEFEK EEDCEKAFFK MDNVLIDDRR IHVDFSQSVA KVKWKGKGGK YTKSDFKEYE KEQDKPPNLV LKDKVKPKQD TKYDLILDEQ AEDSKSSHSH TSKKHKKKTH HCSEEKEDED YMPIKNTNQD IYREMGFGHY EEEESCWEKQ KSEKRDRTQN RSRSRSRERD GHYSNSHKSK YQTDLYERER SKKRDRSRSP KKSKDKEKSK YR.
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 HumanDescription:
VEGF Co-regulated Chemokine 1 Human Recombinant
VEGF coregulated chemokine 1, C-X-C motif chemokine 17, Dendritic cell and monocyte chemokine-like protein, DMC, CXCL17, VCC1, Dcip1, VCC-1, UNQ473.
Product # :
CHM-019Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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- biological activity
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Description
CXCL17 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 98 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 PBS, pH 7.4, containing 3% Trehalose.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by its ability to induce VEGF expression using murine endothelial cells is less than 5.0µg/ml, corresponding to a specific activity of > 200IU/mg.More Info
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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.
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Synonyms
VEGF coregulated chemokine 1, C-X-C motif chemokine 17, Dendritic cell and monocyte chemokine-like protein, DMC, CXCL17, VCC1, Dcip1, VCC-1, UNQ473.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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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.
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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.
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Amino Acid Sequence
SSLNPGVARG HRDRGQASRR WLQEGGQECE CKDWFLRAPR RKFMTVSGLP KKQCPCDHFK GNVKKTRHQR HHRKPNKHSR ACQQFLKQCQ LRSFALPL.
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Background
What is the molecular weight/Mw of CXCL17 HUMAN Protein?
CXCL17 HUMAN Protein has a total Mw of 11.5kDa.
What is the source or expression system of CXCL17 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL17 HUMAN Protein?
CXCL17 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL17 HUMAN Protein?
The ED50 as determined by its ability to induce VEGF expression using murine endothelial cells is less than 5.0µg/ml, corresponding to a specific activity of > 200IU/mg.
What is the amino acid sequence of CXCL17 HUMAN Protein?
SSLNPGVARG HRDRGQASRR WLQEGGQECE CKDWFLRAPR RKFMTVSGLP KKQCPCDHFK GNVKKTRHQR HHRKPNKHSR ACQQFLKQCQ LRSFALPL.
What applications can CXCL17 HUMAN Protein be used in?
CXCL17 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL17 HUMAN Protein?
The endotoxin level is minimal, CXCL17 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 :
ANXA5 HumanDescription:
Annexin A5 Human Recombinant
PP4, ANX5, ENX2, ANXA5, Annexin A5, Annexin-5, Annexin V, Lipocortin V, Endonexin II, Calphobindin I, CBP-I, Placental anticoagulant protein I, PAP-I, Placental anticoagulant protein 4, Thromboplastin inhibitor, Vascular anticoagulant-alpha, VAC-alpha, Anchorin CII.
Product # :
PRO-732Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
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- More Info
Description
ANXA5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 320 amino acids (1-320 a.a.) and having a molecular mass of 35.9 kDa.ANXA5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ANXA5 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
ANXA5 is a member of the annexin family of calcium-dependent phospholipid binding proteins which are involved in membrane-related activity along exocytotic and endocytotic pathways. ANXA5 is a phospholipase A2 and protein kinase C inhibitory protein with calcium channel properties and takes part in cellular signal transduction, inflammation, growth and differentiation. ANXA5 is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. ANXA5 regulates coagulability in the blood stream by binding to phosphatidylserine and sulfatide. ANXA5 protects sinsuoidal endothelial cells from ischemia reperfusion damage. ANXA5 is necessary for normal CFTR chloride channel activity.
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Synonyms
PP4, ANX5, ENX2, ANXA5, Annexin A5, Annexin-5, Annexin V, Lipocortin V, Endonexin II, Calphobindin I, CBP-I, Placental anticoagulant protein I, PAP-I, Placental anticoagulant protein 4, Thromboplastin inhibitor, Vascular anticoagulant-alpha, VAC-alpha, Anchorin CII.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MAQVLRGTVT DFPGFDERAD AETLRKAMKG LGTDEESILT LLTSRSNAQR QEISAAFKTL FGRDLLDDLK SELTGKFEKL IVALMKPSRL YDAYELKHAL KGAGTNEKVL TEIIASRTPE ELRAIKQVYE EEYGSSLEDD VVGDTSGYYQ RMLVVLLQAN RDPDAGIDEA QVEQDAQALF QAGELKWGTD EEKFITIFGT RSVSHLRKVF DKYMTISGFQ IEETIDRETS GNLEQLLLAV VKSIRSIPAY LAETLYYAMK GAGTDDHTLI RVMVSRSEID LFNIRKEFRK NFATSLYSMI KGDTSGDYKK ALLLLCGEDD.
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 :
CALML3 HumanDescription:
Calmodulin Like 3 Human Recombinant
Calmodulin-like protein 3, CaM-like protein, CLP, Calmodulin-related protein NB-1, CALML3.
Product # :
PRO-1323Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
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Description
CALML3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids (1-149 a.a.) and having a molecular mass of 19kDa.CALML3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CALML3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Calmodulin Like 3 (CALML3) is a member of the calmodulin family and contains 4 EF-hand domains. The CALML3 protein may be similar to that of genuine calmodulin and may in fact compete with calmodulin by binding, with different affinities, to cellular substrates. CALML3 protein is expressed in normal mammary, prostate, cervical, and epidermal tissues.
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Synonyms
Calmodulin-like protein 3, CaM-like protein, CLP, Calmodulin-related protein NB-1, CALML3.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMADQLT EEQVTEFKEA FSLFDKDGDG CITTRELGTV MRSLGQNPTE AELRDMMSEI DRDGNGTVDF PEFLGMMARK MKDTDNEEEI REAFRVFDKD GNGFVSAAEL RHVMTRLGEK LSDEEVDEMI RAADTDGDGQ VNYEEFVRVL VSK.
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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Name :
CCDC25 HumanDescription:
Coiled-Coil Domain Containing 25 Human Recombinant
Coiled-coil domain-containing protein 25, CCDC25.
Product # :
PRO-1655Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CCDC25 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (1-208 a.a) and having a molecular mass of 26.9kDa.CCDC25 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CCDC25 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Coiled-Coil Domain Containing 25 (CCDC25) is a 208 amino acid protein belonging to the CCDC25 family.
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Synonyms
Coiled-coil domain-containing protein 25, CCDC25.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMVFYFTS SSVNSSAYTI YMGKDKYENE DLIKHGWPED IWFHVDKLSS AHVYLRLHKG ENIEDIPKEV LMDCAHLVKA NSIQGCKMNN VNVVYTPWSN LKKTADMDVG QIGFHRQKDV KIVTVEKKVN EILNRLEKTK VERFPDLAAE KECRDREERN EKKAQIQEMK KREKEEMKKK REMDELRSYS SLMKVENMSS NQDGNDSDEF M.
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
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- source
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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
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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.
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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.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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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 :
CAMP HumanDescription:
Cathelicidin Antimicrobial Peptide Human Recombinant
CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.
Product # :
PRO-1405Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
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Description
CAMP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (34-173 a.a.) and having a molecular mass of 18.4kDa.CAMP is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
CAMP 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.
More Info
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Introduction
CAMP belongs to the antimicrobial peptide family, contains highly conserved N-terminal signal peptide, a cathelin domain and a structurally variable cationic antimicrobial peptide that produced by extracellular proteolysis from the C-terminus. CAMP has numerous functions besides the antimicrobial activity such as: cell chemotaxis, immune mediator induction and inflammatory response regulation.
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Synonyms
CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQVLSYKE AVLRAIDGIN QRSSDANLYR LLDLDPRPTM DGDPDTPKPV SFTVKETVCP RTTQQSPEDC DFKKDGLVKR CMGTVTLNQA RGSFDISCDK DNKRFALLGD FFRKSKEKIG KEFKRIVQRI KDFLRNLVPR TES.
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.