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1000 results found for “Cystatin”
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Name :
NECTIN1 HumanDescription:
Nectin Cell Adhesion Molecule 1 Human Recombinant
PVRL1, CD111, CLPED1, ED4, HIgR, HVIS, HVEC, Nectin-1, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12.
Product # :
PRO-2648Price :
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Shipped with Ice Packs
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Description
NECTIN1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 334amino acids (31-355a.a) and having a molecular mass of 37.3kDa.NECTIN1 is fused to an 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The NECTIN1 solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Nectin-1, also referred to as ED4, is a poliovirus receptor- related 1 protein is a part of the Nectin family. Nectin-1 endorses cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions among PVRL1/nectin-1 & PVRL4/nectin-4 and among PVRL1/nectin-1 & PVRL3/nectin-3 have been found. Nectin-1 acts as an entry receptor for herpes simplex virus & pseudorabies virus as well. Likewise, Neurite outgrowth-promoting activity has been shown by Nectin-1.
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Synonyms
PVRL1, CD111, CLPED1, ED4, HIgR, HVIS, HVEC, Nectin-1, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12.
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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
ADPQVVQVND SMYGFIGTDV VLHCSFANPL PSVKITQVTW QKSTNGSKQN VAIYNPSMGV SVLAPYRERV EFLRPSFTDG TIRLSRLELE DEGVYICEFA TFPTGNRESQ LNLTVMAKPT NWIEGTQAVL RAKKGQDDKV LVATCTSANG KPPSVVSWET RLKGEAEYQE IRNPNGTVTV ISRYRLVPSR EAHQQSLACI VNYHMDRFKE SLTLNVQYEP EVTIEGFDGN WYLQRMDVKL
TCKADANPPA TEYHWTTLNG SLPKGVEAQN RTLFFKGPIN YSLAGTYICE ATNPIGTRSG QVEVNITEFP YTPSPPEHGR RAGPVPTAHH HHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PMSGDescription:
Pregnant Mare Serum Gonadotropin
Product # :
HOR-272Price :
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Description
PMSG is a complex glycoprotein obtained from the serum of pregnant mares. This 43-63 kda protein is capable of supplementing and being substituted for the follicle stimulating and interstitial cell-stimulating hormone of the anterior pituitary gland in both the male and female. Thus PMSG-Intervet stimulates development of the ovarian follicle in the female.
Source
Serum of pregnant mares.
Formulation
The PMSG was lyophilized with no additives.
More Info
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Introduction
PMSG Hormone is a well know used hormone together with progestogen to increase ovulation just before to artificial insemination. PMSG hormone is a placental glycoprotein produced from the serum of pregnant mares. PMSG comprises of an alfa subunit and a beta subunit. PMSG hormone is secreted from endometrial cups within the pregnant mare uterus aging from 40 to 130 days into their maturation, and once extracted, it can been used to promote artificially estrus in female animals. These assemblies produce PMSG hormone to induce mare's ovarian and repsouctive structures. PMSG can induce the growth of follicles by ovaries and results in ovulatation. PMSG hormone has an about a 4 day half-life of bioactivity in species other than horses. The extended biological activity can cause ovarian stimulation and ovulation. However, PMSG use alone often causes cystic ovarian disease because of the unrestrained ovarian stimulation and due to the sugar molecules which decrease clearance of the hormone. PMSG is more likely to be used than other pituitary hormones due to the extended circulatory half-life. PMSG solely exhibits luteinizing hormone like activity, however in other animal classes it has FSH & LH like activity.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PMSG although stable at room temperature for 3 weeks, should be stored between 2-8°C.
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Solubility
It is recommended to reconstitute the lyophilized PMSG in sterile 18M-cm H2O at a concentration of 1000 IU/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.
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Name :
Resistin MouseDescription:
Resistin Mouse Recombinant
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Product # :
CYT-1034Price :
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Shipped at Room temp
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Description
Resistin Mouse Recombinant produced in E.Coli is a non glycosylated, homodimeric polypeptide chain containing 2 x 95 amino acids and having a total molecular mass of 20.6kDa. The Resistin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrofobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severly suppressed in obesity and is stimulated by several antidiabetic drugs.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression. -
Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Resistin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Resistin Mouse 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 Resistin in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MSSMPLCPID EAIDKKIKQD FNSLFPNAIK NIGLNCWTVS SRGKLASCPE GTAVLSCSCG SACGSWDIRE EKVCHCQCAR IDWTAARCCK LQVAS.
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 :
Activin-A Human ActiveDescription:
Activin-A Human Recombinant, Active
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-145Price :
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Shipped at Room temp
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Description
Active form Activin-A Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.
Source
E.Coli.
Formulation
Human Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
Biological activity is assessed by the ability to induce cytotoxicity of MPC-11 cells and was found to be 8.95ng/ml corresponding to a specific activity of 1.1 x 105 units/mg.
More Info
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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
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Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A 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
Human INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
Title: Research on Activin A Human Recombinant: Molecular Characteristics, Signaling Pathways, Physiological Functions, and Therapeutic Potential
Introduction:
Activin A, a member of the transforming growth factor-beta (TGF-β) superfamily, is a multifunctional cytokine that plays a significant role in various biological processes in the human body. Its involvement in diverse physiological and pathological functions has garnered considerable attention in scientific research. This paper aims to provide an overview of Activin A, encompassing its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential.
Activin A is encoded by the INHBA gene and is produced as a precursor protein that undergoes post-translational modifications to generate the mature form. The mature Activin A protein consists of two β-subunits held together by disulfide bonds. These structural features contribute to its functional properties and interactions with specific receptors.
Upon binding to its cell surface receptors, Activin A triggers intracellular signaling cascades, leading to various cellular responses. Canonical SMAD-dependent pathway as well as non-SMAD pathways, such as MAPK/ERK, PI3K/Akt, and JNK signaling, are activated by Activin A. The intricate network of signaling pathways enables Activin A to regulate diverse biological processes, including cell proliferation, differentiation, apoptosis, and tissue homeostasis.
Activin A exerts its physiological functions in a tissue-specific manner. It plays a critical role in embryonic development, particularly in organogenesis and patterning. Additionally, Activin A is involved in reproductive biology, where it participates in folliculogenesis, spermatogenesis, and hormonal regulation. It also contributes to neural development, immune system modulation, and skeletal homeostasis.
The multifunctional properties of Activin A have positioned it as a potential therapeutic target for various diseases. Its involvement in cancer, neurodegenerative disorders, fibrosis, and reproductive disorders has prompted extensive research to explore its therapeutic potential. Understanding the molecular mechanisms underlying Activin A's actions provides valuable insights for developing innovative therapeutic strategies.
In conclusion, Activin A is a versatile cytokine with diverse roles in human biology. This research aims to deepen our understanding of its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential. By elucidating the complexities of Activin A, we strive to pave the way for novel therapeutic interventions in various human diseases.
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 :
SOST Human, HEKDescription:
Sclerostin Human Recombinant, HEK
Sclerostin, SOST, CDD, VBCH.
Product # :
PRO-2481Price :
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Description
SOST Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 24-213) containing 196 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 22.4kDa (calculated).
Source
HEK293 Cells.
Formulation
SOST filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS and 5 % (w/v) trehalose, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein (BMP) antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is widely expressed at low levels, with highest levels in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.
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Synonyms
Sclerostin, SOST, CDD, VBCH.
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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 one week 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. SOST 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
QGWQAFKNDA TEIIPELGEY PEPPPELENN KTMNRAENGG RPPHHPFETK DVSEYSCREL HFTRYVTDGP CRSAKPVTEL VCSGQCGPAR LLPNAIGRGK WWRPSGPDFR CIPDRYRAQR VQLLCPGGEA PRARKVRLVA SCKCKRLTRF HNQSELKDFG TEAARPQKGR KPRPRARSAK ANQAELENAY HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Inhibin a HumanDescription:
Inhibin Alpha Human Recombinant
Product # :
HOR-303Price :
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Description
Inhibin-Alpha Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 264 amino acids comprising of both A and B chains, having a molecular mass of 33.5 kDa.The Inhibin-Alpha is fused with an amino-terminal hexahistidine tag. The Inhibin-Alpha is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
Inhibin-A alpha chain is supplied in 20mM Tris and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE analysis.
More Info
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Introduction
Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development. -
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.Please avoid freeze thaw cycles.
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Amino Acid Sequence
Alpha chain:
STPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIP PNLSLPVPGAPPTPAQPYSLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI.
Beta Chain:
GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMR
GHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.
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 :
PI3 HumanDescription:
Peptidase Inhibitor 3 Human Recombinant
Peptidase Inhibitor 3 Skin-Derived, Skin-Derived Antileukoproteinase, Protease Inhibitor 3 Skin-Derived (SKALP), WAP Four-Disulfide Core Domain Protein 14, WAP Four-Disulfide Core Domain 14, Elastase-Specific Inhibitor, Protease Inhibitor WAP3, ESI, trappin-2, cementoin, WFDC14, WAP3, elafin, pre-elafin, SKALP, Peptidase Inhibitor 3.
Product # :
PRO-1627Price :
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Description
PI3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (23-117) and having a molecular mass of 12.0kDa.PI3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PI3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
PI3 is an elastase-specific protease inhibitor, which contains a WAP-type four-disulfide core (WFDC) domain, and is thus a member of the WFDC domain family. Most WFDC gene members are localized to chromosome 20q12-q13 in two clusters: centromeric and telomeric. PI3 belongs to the centromeric cluster.
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Synonyms
Peptidase Inhibitor 3 Skin-Derived, Skin-Derived Antileukoproteinase, Protease Inhibitor 3 Skin-Derived (SKALP), WAP Four-Disulfide Core Domain Protein 14, WAP Four-Disulfide Core Domain 14, Elastase-Specific Inhibitor, Protease Inhibitor WAP3, ESI, trappin-2, cementoin, WFDC14, WAP3, elafin, pre-elafin, SKALP, Peptidase Inhibitor 3.
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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 MGSAVTGVPV KGQDTVKGRV PFNGQDPVKG QVSVKGQDKV KAQEPVKGPV STKPGSCPII LIRCAMLNPP NRCLKDTDCP GIKKCCEGSC GMACFVPQ
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 :
CX3CL1 Human, HisDescription:
Fractalkine Human Recombinant (CX3CL1), His Tag
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
Product # :
CHM-360Price :
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Shipped with Ice Packs
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Description
Fractalkine 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 97 amino acids (25-100 a.a.) and having a molecular mass of 10.9kDa. The Fractalkine is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Fractalkine solution (0.5 mg/ml) contains Phosphate Buffered Saline pH7.4 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.
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Synonyms
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
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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 MQHHGVTKCN ITCSKMTSKI PVALLIHYQQ NQASCGKRAI ILETRQHRLF CADPKEQWVK DAMQHLDRQA AALTRNG.
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Background
What is the molecular weight/Mw of CX3CL1 HUMAN, HIS Protein?
CX3CL1 HUMAN, HIS Protein has a total Mw of 10.9kDa.
What is the source or expression system of CX3CL1 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CX3CL1 HUMAN, HIS Protein?
CX3CL1 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CX3CL1 HUMAN, HIS Protein?
The biological functionality of CX3CL1 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CX3CL1 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MQHHGVTKCN ITCSKMTSKI PVALLIHYQQ NQASCGKRAI ILETRQHRLF CADPKEQWVK DAMQHLDRQA AALTRNG.
What applications can CX3CL1 HUMAN, HIS Protein be used in?
CX3CL1 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CX3CL1 HUMAN, HIS Protein?
The endotoxin level is minimal, CX3CL1 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Vimentin BovineDescription:
Bovine Vimentin
Vimentin, Vim, FLJ36605.
Product # :
PRO-525Price :
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Description
Bovine Vimentin protein produced in Bovine Lens, having a molecular weight of 57 kDa.
Source
Bovine Lens.
Formulation
The protein (1mg/ml) was lyophilized from a 1mg/ml solution containing 10mM sodium phosphate pH 7.5, 6M urea, 2mM DTT, 1mM EDTA and 10mM methylammonium chloride.
Purity
Greater than 98.0% as determined by SDS-PAGE.
More Info
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Introduction
Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines. Vimentin is the main intermediate filament protein in mesenchymal cells and is therefore of value in the differential diagnosis of undifferentiated neoplasms.
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Synonyms
Vimentin, Vim, FLJ36605.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bovine Vimentin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BovineVimentin 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 Bovine Vimentin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Reconstitution to filaments
After vimentin is dissolved in 6M urea buffer (see above), protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCl, 2mM dithiothreitol, 10mM Sodium Phosphate, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco''s PBS).- Hatzfeld M. and Franke W.W. (1985). J. Cell Biol. 101, 1826-1841.- Hatzfeld M. et al. (1987). J. Mol. Biol. 197, 237-255.
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 HumanDescription:
Cyclophilin-H Human Recombinant
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-379Price :
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Shipped with Ice Packs
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Description
PPIH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 177 amino acids (1-177) and having a molecular mass of 19.2 kDa. PPIH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1 mg/ml solution containing 1x PBS pH-7.4 10% glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Specific activity is > 220 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
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
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).Please prevent freeze thaw cycles.
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Amino Acid Sequence
MAVANSSPVN PVVFFDVSIG GQEVGRMKIE LFADVVPKTA ENFRQFCTGEFRKDGVPIGY KGSTFHRVIK DFMIQGGDFV NGDGTGVASI YRGPFADENF KLRHSAPGLL SMANSGPSTN GCQFFITCSK CDWLDGKHVV FGKIIDGLLV MRKIENVPTG PNNKPKLPVV ISQCGEM.
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 :
SOSTDC1 HumanDescription:
Sclerostin Domain Containing 1 Human Recombinant
Sclerostin domain-containing protein 1, Ectodermal BMP inhibitor, Ectodin, Uterine sensitization-associated gene 1 protein, USAG-1, SOSTDC1, USAG1, CDA019.
Product # :
PRO-426Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SOSTDC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (24-206 a.a) and having a molecular mass of 23kDa.SOSTDC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SOSTDC1 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
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Introduction
Sclerostin Domain Containing 1 (SOSTDC1) belongs to the sclerostin family and an N-glycosylated, secreted protein with a C-terminal cystine knot-like domain. The SOSTDC1 protein acts as a bone morphogenetic protein (BMP) antagonist. Specifically, SOSTDC1 directly associates with BMPs, prohibiting them from binding their receptors, thus regulating BMP signaling throughout cellular proliferation, differentiation, and programmed cell death. SOSTDC1 may also be involved in the onset of endometrial receptivity for implantation/sensitization for the decidual cell reaction Enhances Wnt signaling and hinders TGF-beta signaling. In addition, SOSTDC1 directly antagonizes the activity of BMP2, BMP4, BMP6 and BMP7 in a dose-dependent manner.
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Synonyms
Sclerostin domain-containing protein 1, Ectodermal BMP inhibitor, Ectodin, Uterine sensitization-associated gene 1 protein, USAG-1, SOSTDC1, USAG1, CDA019.
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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 MGSFKNDATE ILYSHVVKPV PAHPSSNSTL NQARNGGRHF SNTGLDRNTR VQVGCRELRS TKYISDGQCT SISPLKELVC AGECLPLPVL PNWIGGGYGT KYWSRRSSQE WRCVNDKTRT QRIQLQCQDG STRTYKITVV TACKCKRYTR QHNESSHNFE SMSPAKPVQH HRERKRASKS SKHSMS.
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 :
OTOR HumanDescription:
Otoraplin Human Recombinant
Otoraplin, Fibrocyte-derived protein, Melanoma inhibitory activity-like protein, OTOR, MIAL, FDP, MIAL1, MGC126737, MGC126739.
Product # :
CYT-582Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Otoraplin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12.7 kDa.The OTOR is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OTOR protein was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 130mM NaCl.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
OTOR proteins is also known as fibrocyte-derived protein (Fdp) and Melanoma inhibitory activity-like (MIAL). Otoraplin is a member of the melanoma-inhibiting activity gene family. Otoraplin is a secreted 16 kDa globular protein that is expressed in the inner ear by periotic mesenchyme and developing and mature fibrocytes. OTOR is highly homologous to MIA/cartilage-derived retinoic acid-sensitive protein (CD-RAP), which is a cartilage-specific protein that is also expressed in malignant melanoma cells. The 111 amino acid mature human otoraplin contains 1 SH3 domain (46 – 107 amino acids) and a Tyr at position 50 that is reportedly sulfated. Otoraplin takes pasrt in the initiation of periotic mesenchyme chondrogenesis.
Otoraplin is secreted through the Golgi apparatus and plays a role in cartilage development and maintenance. A frequent polymorphism in the translation start codon of OTOR can abolish translation and may be associated with forms of deafness. -
Synonyms
Otoraplin, Fibrocyte-derived protein, Melanoma inhibitory activity-like protein, OTOR, MIAL, FDP, MIAL1, MGC126737, MGC126739.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized OTOR Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OTOR 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 Otoraplin 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
VHGIFMDRLASKKLCADDECVYTISLASAQEDYNAPDCRFINVKKGQQIYVYS
KLVKENGAGEFWAGSVYGDGQDEMGVVGYFPRNLVKEQRVYQEATKEVPTT
DIDFFCE.
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 :
STX11 HumanDescription:
Syntaxin-11 Human Recombinant
Syntaxin-11, STX11, FHL4, HLH4, HPLH4.
Product # :
PRO-1111Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
STX11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 311 amino acids (1-287 a.a) and having a molecular mass of 35.8kDa.STX11 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
STX11 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Syntaxin-11 (STX11) belongs to the t-SNARE family. Syntaxin-11 regulates protein transport between late endosomes and the trans-Golgi network. STX11 interacts with the SNARE proteins SNAP-23 and VAMP. STX11 gene mutations are linked with familial hemophagocytic lymphohistiocytosis.
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Synonyms
Syntaxin-11, STX11, FHL4, HLH4, HPLH4.
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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 MGSHMKDRLA ELLDLSKQYD QQFPDGDDEF DSPHEDIVFE TDHILESLYR DIRDIQDENQ LLVADVKRLG KQNARFLTSM RRLSSIKRDT NSIAKAIKAR GEVIHCKLRA MKELSEAAEA QHGPHSAVAR ISRAQYNALT LTFQRAMHDY NQAEMKQRDN CKIRIQRQLE IMGKEVSGDQ IEDMFEQGKW DVFSENLLAD VKGARAALNE IESRHRELLR LESRIRDVHE LFLQMAVLVE KQADTLNVIE LNVQKTVDYT GQAKAQVRKA VQYEEKNPCR TLCCFCCPCL K.
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 :
CACYBP HumanDescription:
Calcyclin Binding Protein Human Recombinant
S100A6BP, S100A6 Binding Protein, GIG5, PNAS-107, RP1-102G20.6, SIP, CACYBP, hCacyBP, Siah-interacting protein, MGC87971.
Product # :
PRO-831Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CACYBP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 205 amino acids (1-185a.a.) and having a molecular mass of 23.4 kDa. CACYBP protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
CACYBP Human solution containing 20mM Tris HCL pH-8, 1mM DTT, 0.1M NaCl & 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
CACYBP (calcyclin binding protein) participates in calcium-dependent ubiquitination and subsequent proteosomal degradation of target proteins. CACYBP acts as a molecular bridge in ubiquitin E3 complexes. CACYBP is involved in the ubiquitin-mediated degradation of beta-catenin.
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Synonyms
S100A6BP, S100A6 Binding Protein, GIG5, PNAS-107, RP1-102G20.6, SIP, CACYBP, hCacyBP, Siah-interacting protein, MGC87971.
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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 MQQKSQKKAE LLDNEKPAAV VAPITTGYTV KISNYGWDQS DKFVKIYITL TGVHQVPTEN VQVHFTERSF DLLVKNLNGK SYSMIVNNLL KPISVEGSSK KVKTDTVLIL CRKKVENTRW DYLTQVEKEC KEKEKPSYDT ETDPSEGLMN VLKKIYEDGD DDMKRTINKA WVESREKQAK GDTEF.
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 :
CCL28 HumanDescription:
Mucosae-Associated Epithelial Chemokine Human Recombinant (CCL28)
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
Product # :
CHM-353Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CCL28 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 108 amino acids and having a molecular mass of 12.3 kDa. The CCL28 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM PBS and 150mM 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 lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues. -
Synonyms
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CCL28 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL28 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 CCL28 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
SEAILPIASS CCTEVSHHIS RRLLERVNMC RIQRADGDCD LAAVILHVKR RRICVSPHNH TVKQWMKVQA AKKNGKGNVC HRKKHHGKRN SNRAHQGKHE TYGHKTPY.
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Background
What is the molecular weight/Mw of CCL28 HUMAN Protein?
CCL28 HUMAN Protein has a total Mw of 12.3kDa.
What is the source or expression system of CCL28 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL28 HUMAN Protein?
CCL28 HUMAN Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL28 HUMAN Protein?
Determined by its ability to chemoattract human lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CCL28 HUMAN Protein?
SEAILPIASS CCTEVSHHIS RRLLERVNMC RIQRADGDCD LAAVILHVKR RRICVSPHNH TVKQWMKVQA AKKNGKGNVC HRKKHHGKRN SNRAHQGKHE TYGHKTPY.
What applications can CCL28 HUMAN Protein be used in?
CCL28 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL28 HUMAN Protein?
The endotoxin level is minimal, CCL28 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 :
CDKN3 HumanDescription:
Cyclin-Dependent Kinase Inhibitor 3 Human Recombinant
Cyclin-dependent kinase inhibitor 3, CDK2-associated dual-specificity phosphatase, Cyclin-dependent kinase interactor 1, Cyclin-dependent kinase-interacting protein 2, Kinase-associated phosphatase, KAP, CDI1, CIP2, KAP1, FLJ25787, MGC70625, CDKN3.
Product # :
PKA-336Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CDKN3 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 232 amino acids (1-212 a.a.) and having a molecular mass of 25.9kDa. The CDKN3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CDKN3 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 40% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cyclin-dependent kinase inhibitor 3 (CDKN3) is a member of the dual specificity protein phosphatase family. CDKN3 was identified as a cyclin-dependent kinase inhibitor, and was shown to interact with, and dephosphorylate CDK2 kinase, consequently prevent the activation of CDK2 kinase. In addition CDKN3 is important in cell cycle regulation. The CDKN3 gene was reported to be deleted, mutated, or overexpressed in several kinds of cancers.
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Synonyms
Cyclin-dependent kinase inhibitor 3, CDK2-associated dual-specificity phosphatase, Cyclin-dependent kinase interactor 1, Cyclin-dependent kinase-interacting protein 2, Kinase-associated phosphatase, KAP, CDI1, CIP2, KAP1, FLJ25787, MGC70625, CDKN3.
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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 MKPPSSIQTS EFDSSDEEPI EDEQTPIHIS WLSLSRVNCS QFLGLCALPG CKFKDVRRNV QKDTEELKSC GIQDIFVFCT RGELSKYRVP NLLDLYQQCG IITHHHPIAD GGTPDIASCC EIMEELTTCL KNYRKTLIHC YGGLGRSCLV AACLLLYLSD TISPEQAIDS LRDLRGSGAI QTIKQYNYLH EFRDKLAAHL SSRDSQSRSV SR.
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 :
Desmin ChickenDescription:
Desmin Chicken Gizzard
Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.
Product # :
PRO-2783Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Desmin Chicken having a calculated molecular mass of 53 kDa, pI-5.4.
Source
Chicken gizzard.
Formulation
Desmin was lyophilized from a 1mg/ml solution containing 10 mM sodium phosphate buffer pH 7.5, 6M urea, 1mM EDTA, 2mM DTT and 10mM methylammonium chloride.
Purity
Greater than 98.0% as determined by SDS-PAGE.
More Info
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Synonyms
Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Desmin between 2-8°C, do not freeze. Upon reconstitution Desmin should be stored at -20°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Desmin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Desmin, an intermediate filament protein, plays a fundamental role in maintaining the structural integrity and function of muscle cells. While extensive research has been conducted on desmin in mammals, the study of desmin in chickens is an emerging area with considerable potential for advancing our understanding of muscle biology. Chickens are valuable model organisms for studying muscle development, growth, and regeneration due to their relatively simple muscular system and economic significance in poultry production. This research aims to provide a comprehensive exploration of desmin in chickens, shedding light on its functions and implications for muscle structure and function.
The primary objective of this research is to elucidate the role of desmin in chicken muscle structure and development. In vitro and in vivo experiments, utilizing chicken cell cultures and embryonic models, will be conducted to investigate how desmin contributes to the organization of muscle fibers, sarcomere assembly, and myofibrillogenesis. Understanding these mechanisms is fundamental for deciphering the complexities of muscle development in chickens.
The second objective is to assess the clinical and economic relevance of desmin in poultry production. Studies involving broiler chickens will be conducted to evaluate the impact of desmin mutations or variations on muscle growth, meat quality, and disease susceptibility. These investigations may provide valuable insights into potential strategies for enhancing poultry production efficiency and meat quality.
The third objective is to explore the potential applications of desmin in biotechnology and tissue engineering. Research will investigate the use of desmin-expressing chicken cells as models for studying muscle-related diseases and for developing tissue engineering approaches for muscle repair and regeneration.
By delving into the functions and roles of desmin in chickens, this research aims to expand our knowledge of muscle biology, its implications for poultry production, and its potential applications in biotechnology and regenerative medicine.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin qA Human, PEGDescription:
Leptin Quadruple Antagonist Pegylated Human Recombinant
Product # :
CYT-1251Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Pegylated Quadruple Antagonist Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and an additional Ala at N-terminus acids. The Human Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Human Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Human Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Human Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated human leptin antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated human leptin antagonist), resulting mainly from increased food intake. The in vivo activity of human pegylated super leptin antagonist was compared to that of human pegylated leptin antagonist is 9-27 fold higher.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Human Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of Human pegylated leptin antagonist and filter sterilization Human pegylated leptin antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Human Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin is a~16 kDa protein which is encoded by the obese gene. Leptin is a hormone which participates in regulating body weight, reproductive function and metabolism. leptin is expressed predominantly by adipocytes, which supports the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
OstreolysinDescription:
Ostreolysin Pleurotus Ostreatus Recombinant
Product # :
PRO-2600Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Pleurotus Ostreatus Ostreolysin Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 137 amino acids and having a molecular mass of 15 kDa. The Ostreolysin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Ostreolysin protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Ostreolysin has potent anti-carcinogenic activity in several colon cancer cell lines.
More Info
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Introduction
Ostreolysin is extracted from Pleurotus ostreatus (oyster mushroom). It is a pore forming protein, which contains a lytic part to both cholesterol and sphingomyelin containing membranes. Because of their cholesterol content and the appearance of ostreolysin in the detergent resistant membranes, ostreolysin is cytotoxic towards the ovary cells of Chinese hamster. It seems that Ostreolysin spots a rich lipid cholesterol phase, presumably the liquid ordered phase.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Pleurotus Ostreatus Ostreolysin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon C between 2-7 days and for future use reconstituted Ostreolysin should be stored at 4°C below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Ostreolysin in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The N-terminal amino sequence is Ala-Tyr-Ala-Gln-Trp-Val.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 2.64 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNA-man computer analysis program.
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 :
Cardiac Actin BovineDescription:
Cardiac Actin Bovine
Actin alpha cardiac muscle 1, Alpha-cardiac actin, ACTC1, ACTC.
Product # :
PRO-519Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
- source
- formulation
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- More Info
Description
Ultra pure Cardiac Actin having a Molecular mass of 43,000 dalton.
Source
Bovine Heart.
Formulation
The protein was lyophilized from a 1mg/ml solution containing 10mM Tris-acetate buffer pH 8.0, 0.2mM CaCl2, 0.2mM ATP, 1mM DTT and 0.5% SDS.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Alpha-cardiac actin belongs to the actin family which is comprised of three main groups of actin isoforms, alpha, beta, and gamma. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. Defects in the cardiac actin have been associated with idiopathic dilated cardiomyopathy (IDC) and familial hypertrophic cardiomyopathy (FHC).
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Synonyms
Actin alpha cardiac muscle 1, Alpha-cardiac actin, ACTC1, ACTC.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Cardiac-Actin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Cardiac Actin 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 Cardiac Actin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Applications
Protein standard in 1D and 2D SDS gelelectrophoresis
Immunoassays
Immunization.
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 :
LL-37Description:
LL-37
LL37, antibacterial protein LL-37, cathelicidin LL 37, camp.
Product # :
HOR-041Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
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- purity
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Description
LL-37 Synthetic is a single, non-glycosylated polypeptide chain containing 37 amino acids, having a molecular mass of 4493 Dalton and a Molecular formula of C205H340N60O53.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
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Synonyms
LL37, antibacterial protein LL-37, cathelicidin LL 37, camp.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LL-37 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LL-37 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 LL-37 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
H-Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser-OH.
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Background
LL-37, a prominent member of the human cathelicidin family, has emerged as a pivotal host defense peptide with diverse biological functions. This research paper aims to provide a comprehensive analysis of LL-37, elucidating its biochemical properties, antimicrobial activity, immunomodulatory effects, and potential therapeutic applications.
LL-37, derived from the precursor protein hCAP18, plays a crucial role in innate immunity and host defense against microbial pathogens. Beyond its well-established antimicrobial properties, LL-37 exhibits various immunomodulatory effects, making it an intriguing target for therapeutic interventions (Lai & Gallo, 2009). This paper aims to delve into the complexities of LL-37, uncovering its multifaceted nature and potential clinical applications.
LL-37 is a cationic peptide characterized by a helical structure that facilitates its interaction with microbial membranes. Its amphipathic nature enables it to penetrate microbial membranes, leading to disruption and subsequent cell death (Zaiou, 2007). Additionally, LL-37 can undergo proteolytic processing to release smaller bioactive fragments with distinct functions (Bowdish et al., 2005).
LL-37's antimicrobial activity extends beyond direct microbial killing. It also exhibits immunomodulatory effects, stimulating the recruitment of immune cells and promoting the clearance of pathogens through phagocytosis (Scott et al., 2002). Furthermore, LL-37 can neutralize endotoxins, reducing inflammation caused by microbial products (Davidson et al., 2004).
LL-37 possesses immunomodulatory properties that influence various immune cells, including neutrophils, macrophages, dendritic cells, and lymphocytes (Nagaoka et al., 2001). It can promote the differentiation and maturation of immune cells, modulate cytokine production, and contribute to wound healing and tissue repair (van Harten et al., 2018).
The multifunctional nature of LL-37 renders it a promising candidate for various therapeutic applications. LL-37-based therapies are being explored in wound healing, infectious diseases, and immune-related disorders (Pena et al., 2014). Furthermore, LL-37 has shown potential as a vaccine adjuvant, enhancing the immune response to antigens (Howell et al., 2018).
LL-37's diverse roles in immunity and host defense warrant further research to unravel its precise mechanisms of action and potential applications in clinical medicine. As we deepen our understanding of LL-37's complexities, its therapeutic potential continues to expand, offering exciting prospects for the future.
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 :
Leptin tA Human, PEGDescription:
Leptin Antagonist Triple Mutant Human Recombinant, Pegylated
Product # :
CYT-702Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
- source
- formulation
- purity
- biological activity
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Description
Pegylated Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 35.6kDa, Leptin was mutated, resulting in L39A/D40A/F41A. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Leptin Antagonist Triple Mutant Human Recombinant is Mono-Pegylated with 20kDa PEG and was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake. Its in vivo activity compared to that of PEG-MLA is 9-27 fold higher.More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PEG-SHLA although stable at room temperature for several weeks, should be stored desiccated below - 20C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml of PEG-SHLA and filter sterilization mLEP mutant can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant pegylated Human Recombinant in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CSN2 HumanDescription:
Casein Beta Human Recombinant
Beta-casein, CSN2, CASB.
Product # :
PRO-1047Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CSN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (16-226 a.a.) and having a molecular mass of 26.6kDa.CSN2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CSN2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.5M NaCl, 0.25M imidazole, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Beta-casein precursor (CSN2) is a member of the beta-casein family. CSN2 has an imperative role in determination of the surface properties of the casein micelles. CSN2 is specific to mammary glands and is secreted in milk.
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Synonyms
Beta-casein, CSN2, CASB.
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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 MGSHMRETIE SLSSSEESIT EYKQKVEKVK HEDQQQGEDE HQDKIYPSFQ PQPLIYPFVE PIPYGFLPQN ILPLAQPAVV LPVPQPEIME VPKAKDTVYT KGRVMPVLKS PTIPFFDPQI PKLTDLENLH LPLPLLQPLM QQVPQPIPQT LALPPQPLWS
VPQPKVLPIP QQVVPYPQRA VPVQALLLNQ ELLLNPTHQI YPVTQPLAPV HNPISV.
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 :
STMN2 HumanDescription:
Stathmin Like-2 Human Recombinant
SCG10, STMB2, SCGN10, AI159727, STMN-2, Stathmin-2, Superior cervical ganglion-10 protein, Protein SCG10, STMN2, SGC10, stathmin-like 2.
Product # :
PRO-752Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
- purity
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Description
Recombinant Human Stathmin Like-2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 142 amino acids (39-179 a.a) and having a molecular mass of 16.4 kDa. STMN2 is purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The STMN2 protein solution contains 50mM MES, pH-6.0, 0.1mM PMSF, 1 mM EDTA and 10% Glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
STMN2 is a neuronal growth-associated protein which shares a majority of its amino acid sequence with the phosphoprotein stathmin. STMN2 is involved in neuronal differentiation and in modulating membrane interaction with the cytoskeleton through neurite outgrowth. STMN2 is necessary for maintaining the anchorage-independent growth state of beta-catenin/TCF-activated hepatoma cells. SCG10 is a novel indicator of osteogenesis and osteoblast that takes part in the regulation of the adipocyte/osteoblast balance. STMN2 plays a role as an effector downstream of Rnd1 to regulate axon extensions by modulating microtubule organization.
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Synonyms
SCG10, STMB2, SCGN10, AI159727, STMN-2, Stathmin-2, Superior cervical ganglion-10 protein, Protein SCG10, STMN2, SGC10, stathmin-like 2.
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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
MDMEVKQINK RASGQAFELI LKPPSPISEA PRTLASPKKK DLSLEEIQKK LEAAEERRKS QEAQVLKQLA EKREHEREVL QKALEENNNF SKMAEEKLIL KMEQIKENRE ANLAAIIERL QEKERHAAEV RRNKELQVEL SG.
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.